---
_id: '10336'
abstract:
- lang: eng
text: Biological membranes can dramatically accelerate the aggregation of normally
soluble protein molecules into amyloid fibrils and alter the fibril morphologies,
yet the molecular mechanisms through which this accelerated nucleation takes place
are not yet understood. Here, we develop a coarse-grained model to systematically
explore the effect that the structural properties of the lipid membrane and the
nature of protein–membrane interactions have on the nucleation rates of amyloid
fibrils. We identify two physically distinct nucleation pathways—protein-rich
and lipid-rich—and quantify how the membrane fluidity and protein–membrane affinity
control the relative importance of those molecular pathways. We find that the
membrane’s susceptibility to reshaping and being incorporated into the fibrillar
aggregates is a key determinant of its ability to promote protein aggregation.
We then characterize the rates and the free-energy profile associated with this
heterogeneous nucleation process, in which the surface itself participates in
the aggregate structure. Finally, we compare quantitatively our data to experiments
on membrane-catalyzed amyloid aggregation of α-synuclein, a protein implicated
in Parkinson’s disease that predominately nucleates on membranes. More generally,
our results provide a framework for understanding macromolecular aggregation on
lipid membranes in a broad biological and biotechnological context.
acknowledgement: We thank T. C. T. Michaels for reading the manuscript. This work
was supported by the Academy of Medical Science (J.K. and A.Š.), the Cambridge Center
for Misfolding Diseases (T.P.J.K.), the Biotechnology and Biological Sciences Research
Council (T.P.J.K.), the Frances and Augustus Newman Foundation (T.P.J.K.), the European
Research Council Grant PhysProt Agreement 337969, the Wellcome Trust (A.Š. and T.P.J.K.),
the Royal Society (A.Š.), the Medical Research Council (J.K. and A.Š.), and the
UK Materials and Molecular Modeling Hub for computational resources, which is partially
funded by Engineering and Physical Sciences Research Council Grant EP/P020194/1.
article_processing_charge: No
article_type: original
author:
- first_name: Johannes
full_name: Krausser, Johannes
last_name: Krausser
- first_name: Tuomas P. J.
full_name: Knowles, Tuomas P. J.
last_name: Knowles
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
citation:
ama: Krausser J, Knowles TPJ, Šarić A. Physical mechanisms of amyloid nucleation
on fluid membranes. Proceedings of the National Academy of Sciences. 2020;117(52):33090-33098.
doi:10.1073/pnas.2007694117
apa: Krausser, J., Knowles, T. P. J., & Šarić, A. (2020). Physical mechanisms
of amyloid nucleation on fluid membranes. Proceedings of the National Academy
of Sciences. National Academy of Sciences. https://doi.org/10.1073/pnas.2007694117
chicago: Krausser, Johannes, Tuomas P. J. Knowles, and Anđela Šarić. “Physical Mechanisms
of Amyloid Nucleation on Fluid Membranes.” Proceedings of the National Academy
of Sciences. National Academy of Sciences, 2020. https://doi.org/10.1073/pnas.2007694117.
ieee: J. Krausser, T. P. J. Knowles, and A. Šarić, “Physical mechanisms of amyloid
nucleation on fluid membranes,” Proceedings of the National Academy of Sciences,
vol. 117, no. 52. National Academy of Sciences, pp. 33090–33098, 2020.
ista: Krausser J, Knowles TPJ, Šarić A. 2020. Physical mechanisms of amyloid nucleation
on fluid membranes. Proceedings of the National Academy of Sciences. 117(52),
33090–33098.
mla: Krausser, Johannes, et al. “Physical Mechanisms of Amyloid Nucleation on Fluid
Membranes.” Proceedings of the National Academy of Sciences, vol. 117,
no. 52, National Academy of Sciences, 2020, pp. 33090–98, doi:10.1073/pnas.2007694117.
short: J. Krausser, T.P.J. Knowles, A. Šarić, Proceedings of the National Academy
of Sciences 117 (2020) 33090–33098.
date_created: 2021-11-25T15:07:09Z
date_published: 2020-12-16T00:00:00Z
date_updated: 2021-11-25T15:35:58Z
day: '16'
doi: 10.1073/pnas.2007694117
extern: '1'
external_id:
pmid:
- '33328273'
intvolume: ' 117'
issue: '52'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://www.biorxiv.org/content/10.1101/2019.12.22.886267v2
month: '12'
oa: 1
oa_version: Published Version
page: 33090-33098
pmid: 1
publication: Proceedings of the National Academy of Sciences
publication_identifier:
eissn:
- 1091-6490
issn:
- 0027-8424
publication_status: published
publisher: National Academy of Sciences
quality_controlled: '1'
scopus_import: '1'
status: public
title: Physical mechanisms of amyloid nucleation on fluid membranes
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 117
year: '2020'
...
---
OA_place: publisher
OA_type: hybrid
_id: '10341'
abstract:
- lang: eng
text: Tracing the motion of macromolecules, viruses, and nanoparticles adsorbed
onto cell membranes is currently the most direct way of probing the complex dynamic
interactions behind vital biological processes, including cell signalling, trafficking,
and viral infection. The resulting trajectories are usually consistent with some
type of anomalous diffusion, but the molecular origins behind the observed anomalous
behaviour are usually not obvious. Here we use coarse-grained molecular dynamics
simulations to help identify the physical mechanisms that can give rise to experimentally
observed trajectories of nanoscopic objects moving on biological membranes. We
find that diffusion on membranes of high fluidities typically results in normal
diffusion of the adsorbed nanoparticle, irrespective of the concentration of receptors,
receptor clustering, or multivalent interactions between the particle and membrane
receptors. Gel-like membranes on the other hand result in anomalous diffusion
of the particle, which becomes more pronounced at higher receptor concentrations.
This anomalous diffusion is characterised by local particle trapping in the regions
of high receptor concentrations and fast hopping between such regions. The normal
diffusion is recovered in the limit where the gel membrane is saturated with receptors.
We conclude that hindered receptor diffusivity can be a common reason behind the
observed anomalous diffusion of viruses, vesicles, and nanoparticles adsorbed
on cell and model membranes. Our results enable direct comparison with experiments
and offer a new route for interpreting motility experiments on cell membranes.
acknowledgement: We thank Jessica McQuade for her input at the start of the project.
We acknowledge support from the ERASMUS Placement Programme (V. E. D.), the UCL
Institute for the Physics of Living Systems (V. E. D. and A. Š.), the UCL Global
Engagement Fund (L. M. C. J.), and the Royal Society (A. Š.).
article_processing_charge: No
article_type: original
author:
- first_name: V. E.
full_name: Debets, V. E.
last_name: Debets
- first_name: L. M. C.
full_name: Janssen, L. M. C.
last_name: Janssen
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
citation:
ama: Debets VE, Janssen LMC, Šarić A. Characterising the diffusion of biological
nanoparticles on fluid and cross-linked membranes. Soft Matter. 2020;16(47):10628-10639.
doi:10.1039/d0sm00712a
apa: Debets, V. E., Janssen, L. M. C., & Šarić, A. (2020). Characterising the
diffusion of biological nanoparticles on fluid and cross-linked membranes. Soft
Matter. Royal Society of Chemistry. https://doi.org/10.1039/d0sm00712a
chicago: Debets, V. E., L. M. C. Janssen, and Anđela Šarić. “Characterising the
Diffusion of Biological Nanoparticles on Fluid and Cross-Linked Membranes.” Soft
Matter. Royal Society of Chemistry, 2020. https://doi.org/10.1039/d0sm00712a.
ieee: V. E. Debets, L. M. C. Janssen, and A. Šarić, “Characterising the diffusion
of biological nanoparticles on fluid and cross-linked membranes,” Soft Matter,
vol. 16, no. 47. Royal Society of Chemistry, pp. 10628–10639, 2020.
ista: Debets VE, Janssen LMC, Šarić A. 2020. Characterising the diffusion of biological
nanoparticles on fluid and cross-linked membranes. Soft Matter. 16(47), 10628–10639.
mla: Debets, V. E., et al. “Characterising the Diffusion of Biological Nanoparticles
on Fluid and Cross-Linked Membranes.” Soft Matter, vol. 16, no. 47, Royal
Society of Chemistry, 2020, pp. 10628–39, doi:10.1039/d0sm00712a.
short: V.E. Debets, L.M.C. Janssen, A. Šarić, Soft Matter 16 (2020) 10628–10639.
date_created: 2021-11-26T06:29:41Z
date_published: 2020-10-06T00:00:00Z
date_updated: 2024-10-16T12:53:17Z
day: '06'
doi: 10.1039/d0sm00712a
extern: '1'
external_id:
pmid:
- '33084724'
intvolume: ' 16'
issue: '47'
keyword:
- condensed matter physics
- general chemistry
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://www.biorxiv.org/content/10.1101/2020.05.01.071761v1
month: '10'
oa: 1
oa_version: Published Version
page: 10628-10639
pmid: 1
publication: Soft Matter
publication_identifier:
issn:
- 1744-683X
- 1744-6848
publication_status: published
publisher: Royal Society of Chemistry
quality_controlled: '1'
scopus_import: '1'
status: public
title: Characterising the diffusion of biological nanoparticles on fluid and cross-linked
membranes
type: journal_article
user_id: 0043cee0-e5fc-11ee-9736-f83bc23afbf0
volume: 16
year: '2020'
...
---
DOAJ_listed: '1'
OA_place: publisher
OA_type: gold
_id: '10342'
abstract:
- lang: eng
text: The blood-brain barrier is made of polarized brain endothelial cells (BECs)
phenotypically conditioned by the central nervous system (CNS). Although transport
across BECs is of paramount importance for nutrient uptake as well as ridding
the brain of waste products, the intracellular sorting mechanisms that regulate
successful receptor-mediated transcytosis in BECs remain to be elucidated. Here,
we used a synthetic multivalent system with tunable avidity to the low-density
lipoprotein receptor–related protein 1 (LRP1) to investigate the mechanisms of
transport across BECs. We used a combination of conventional and super-resolution
microscopy, both in vivo and in vitro, accompanied with biophysical modeling of
transport kinetics and membrane-bound interactions to elucidate the role of membrane-sculpting
protein syndapin-2 on fast transport via tubule formation. We show that high-avidity
cargo biases the LRP1 toward internalization associated with fast degradation,
while mid-avidity augments the formation of syndapin-2 tubular carriers promoting
a fast shuttling across.
acknowledgement: 'Funding: G.B. thanks the ERC for the starting grant (MEViC 278793)
and consolidator award (CheSSTaG 769798), EPSRC/BTG Healthcare Partnership (EP/I001697/1),
EPSRC Established Career Fellowship (EP/N026322/1), EPSRC/SomaNautix Healthcare
Partnership EP/R024723/1, and Children with Cancer UK for the research project (16-227).
X.T. and G.B. thank that Anhui 100 Talent program for facilitating data sharing
and research visits. A.D.-C. and L.R. acknowledge the Royal Society for a Newton
fellowship and the Marie Skłodowska-Curie Actions for a European Fellowship. Author
contributions: X.T. prepared and characterized POs, performed all the fast imaging
in both conventional and STED microscopy, set up the initial BBB model, encapsulated
the PtA2 in POs, and supervised the PtA2-PO animal work. D.M.L. prepared and characterized
POs; performed all the permeability studies, PLA assays, WB and associated data
analysis, and part of the colocalization assays; and performed experiments with
the shRNA for knockdown of syndapin-2. E.S. prepared and characterized POs and performed
part of colocalization assays and Cy7-labeled PO animal experiments. S.N. prepared
and characterized POs and performed part of the colocalization and inhibition assays.
G.F. designed, performed, and analyzed the agent-based simulations of transcytosis.
J.F. designed the image-based algorithm to analyze the PLA data. D.M. prepared and
characterized POs and helped with Cy7-labeled PO animal experiments. A.A. performed
TEM imaging of the POs. A.P. and A.D.-C. synthesized the dye- and peptide-functionalized
and pristine copolymers. M.V., L.H.-K., and A.Š. designed, performed, and analyzed
the MD simulations. Z.Z. supervised and supported STED imaging. P.X., B.F., and
Y.T. synthesized and characterized the PtA2 compound. L.L. performed some of the
animal work. L.R. supported and helped with the BBB characterization. G.B. analyzed
all fast imaging and supervised and coordinated the overall work. X.T., D.M.L.,
E.S., and G.B. wrote the manuscript. Competing interests: The authors declare that
part of the work is associated with the UCL spin-out company SomaNautix Ltd. Data
and materials availability: All data needed to evaluate the conclusions in the paper
are present in the paper and/or the Supplementary Materials. Additional data related
to this paper may be requested from the authors.'
article_number: 'eabc4397 '
article_processing_charge: No
article_type: original
author:
- first_name: Xiaohe
full_name: Tian, Xiaohe
last_name: Tian
- first_name: Diana M.
full_name: Leite, Diana M.
last_name: Leite
- first_name: Edoardo
full_name: Scarpa, Edoardo
last_name: Scarpa
- first_name: Sophie
full_name: Nyberg, Sophie
last_name: Nyberg
- first_name: Gavin
full_name: Fullstone, Gavin
last_name: Fullstone
- first_name: Joe
full_name: Forth, Joe
last_name: Forth
- first_name: Diana
full_name: Matias, Diana
last_name: Matias
- first_name: Azzurra
full_name: Apriceno, Azzurra
last_name: Apriceno
- first_name: Alessandro
full_name: Poma, Alessandro
last_name: Poma
- first_name: Aroa
full_name: Duro-Castano, Aroa
last_name: Duro-Castano
- first_name: Manish
full_name: Vuyyuru, Manish
last_name: Vuyyuru
- first_name: Lena
full_name: Harker-Kirschneck, Lena
last_name: Harker-Kirschneck
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Zhongping
full_name: Zhang, Zhongping
last_name: Zhang
- first_name: Pan
full_name: Xiang, Pan
last_name: Xiang
- first_name: Bin
full_name: Fang, Bin
last_name: Fang
- first_name: Yupeng
full_name: Tian, Yupeng
last_name: Tian
- first_name: Lei
full_name: Luo, Lei
last_name: Luo
- first_name: Loris
full_name: Rizzello, Loris
last_name: Rizzello
- first_name: Giuseppe
full_name: Battaglia, Giuseppe
last_name: Battaglia
citation:
ama: 'Tian X, Leite DM, Scarpa E, et al. On the shuttling across the blood-brain
barrier via tubule formation: Mechanism and cargo avidity bias. Science Advances.
2020;6(48). doi:10.1126/sciadv.abc4397'
apa: 'Tian, X., Leite, D. M., Scarpa, E., Nyberg, S., Fullstone, G., Forth, J.,
… Battaglia, G. (2020). On the shuttling across the blood-brain barrier via tubule
formation: Mechanism and cargo avidity bias. Science Advances. American
Association for the Advancement of Science. https://doi.org/10.1126/sciadv.abc4397'
chicago: 'Tian, Xiaohe, Diana M. Leite, Edoardo Scarpa, Sophie Nyberg, Gavin Fullstone,
Joe Forth, Diana Matias, et al. “On the Shuttling across the Blood-Brain Barrier
via Tubule Formation: Mechanism and Cargo Avidity Bias.” Science Advances.
American Association for the Advancement of Science, 2020. https://doi.org/10.1126/sciadv.abc4397.'
ieee: 'X. Tian et al., “On the shuttling across the blood-brain barrier via
tubule formation: Mechanism and cargo avidity bias,” Science Advances,
vol. 6, no. 48. American Association for the Advancement of Science, 2020.'
ista: 'Tian X, Leite DM, Scarpa E, Nyberg S, Fullstone G, Forth J, Matias D, Apriceno
A, Poma A, Duro-Castano A, Vuyyuru M, Harker-Kirschneck L, Šarić A, Zhang Z, Xiang
P, Fang B, Tian Y, Luo L, Rizzello L, Battaglia G. 2020. On the shuttling across
the blood-brain barrier via tubule formation: Mechanism and cargo avidity bias.
Science Advances. 6(48), eabc4397.'
mla: 'Tian, Xiaohe, et al. “On the Shuttling across the Blood-Brain Barrier via
Tubule Formation: Mechanism and Cargo Avidity Bias.” Science Advances,
vol. 6, no. 48, eabc4397, American Association for the Advancement of Science,
2020, doi:10.1126/sciadv.abc4397.'
short: X. Tian, D.M. Leite, E. Scarpa, S. Nyberg, G. Fullstone, J. Forth, D. Matias,
A. Apriceno, A. Poma, A. Duro-Castano, M. Vuyyuru, L. Harker-Kirschneck, A. Šarić,
Z. Zhang, P. Xiang, B. Fang, Y. Tian, L. Luo, L. Rizzello, G. Battaglia, Science
Advances 6 (2020).
date_created: 2021-11-26T06:40:28Z
date_published: 2020-11-27T00:00:00Z
date_updated: 2024-10-16T12:56:52Z
day: '27'
ddc:
- '611'
doi: 10.1126/sciadv.abc4397
extern: '1'
external_id:
pmid:
- '33246953'
file:
- access_level: open_access
checksum: 3ba2eca975930cdb0b1ce1ae876885a7
content_type: application/pdf
creator: cchlebak
date_created: 2021-11-26T06:50:09Z
date_updated: 2021-11-26T06:50:09Z
file_id: '10343'
file_name: 2020_SciAdv_Tian.pdf
file_size: 10381298
relation: main_file
success: 1
file_date_updated: 2021-11-26T06:50:09Z
has_accepted_license: '1'
intvolume: ' 6'
issue: '48'
keyword:
- multidisciplinary
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://www.biorxiv.org/content/10.1101/2020.04.04.025866v1
month: '11'
oa: 1
oa_version: Published Version
pmid: 1
publication: Science Advances
publication_identifier:
issn:
- 2375-2548
publication_status: published
publisher: American Association for the Advancement of Science
quality_controlled: '1'
scopus_import: '1'
status: public
title: 'On the shuttling across the blood-brain barrier via tubule formation: Mechanism
and cargo avidity bias'
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 0043cee0-e5fc-11ee-9736-f83bc23afbf0
volume: 6
year: '2020'
...
---
OA_place: publisher
OA_type: hybrid
_id: '10344'
abstract:
- lang: eng
text: In this study, we investigate the role of the surface patterning of nanostructures
for cell membrane reshaping. To accomplish this, we combine an evolutionary algorithm
with coarse-grained molecular dynamics simulations and explore the solution space
of ligand patterns on a nanoparticle that promote efficient and reliable cell
uptake. Surprisingly, we find that in the regime of low ligand number the best-performing
structures are characterized by ligands arranged into long one-dimensional chains
that pattern the surface of the particle. We show that these chains of ligands
provide particles with high rotational freedom and they lower the free energy
barrier for membrane crossing. Our approach reveals a set of nonintuitive design
rules that can be used to inform artificial nanoparticle construction and the
search for inhibitors of viral entry.
acknowledgement: We acknowledge support from EPSRC (J. C. F.), MRC (B. B. and A. Š.),
the ERC StG 802960 “NEPA” (J. K. and A. Š.), the Royal Society (A. Š.), and the
United Kingdom Materials and Molecular Modelling Hub for computational resources,
which is partially funded by EPSRC (EP/P020194/1).
article_number: '228101'
article_processing_charge: No
article_type: original
author:
- first_name: Joel C.
full_name: Forster, Joel C.
last_name: Forster
- first_name: Johannes
full_name: Krausser, Johannes
last_name: Krausser
- first_name: Manish R.
full_name: Vuyyuru, Manish R.
last_name: Vuyyuru
- first_name: Buzz
full_name: Baum, Buzz
last_name: Baum
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
citation:
ama: Forster JC, Krausser J, Vuyyuru MR, Baum B, Šarić A. Exploring the design rules
for efficient membrane-reshaping nanostructures. Physical Review Letters.
2020;125(22). doi:10.1103/physrevlett.125.228101
apa: Forster, J. C., Krausser, J., Vuyyuru, M. R., Baum, B., & Šarić, A. (2020).
Exploring the design rules for efficient membrane-reshaping nanostructures. Physical
Review Letters. American Physical Society. https://doi.org/10.1103/physrevlett.125.228101
chicago: Forster, Joel C., Johannes Krausser, Manish R. Vuyyuru, Buzz Baum, and
Anđela Šarić. “Exploring the Design Rules for Efficient Membrane-Reshaping Nanostructures.”
Physical Review Letters. American Physical Society, 2020. https://doi.org/10.1103/physrevlett.125.228101.
ieee: J. C. Forster, J. Krausser, M. R. Vuyyuru, B. Baum, and A. Šarić, “Exploring
the design rules for efficient membrane-reshaping nanostructures,” Physical
Review Letters, vol. 125, no. 22. American Physical Society, 2020.
ista: Forster JC, Krausser J, Vuyyuru MR, Baum B, Šarić A. 2020. Exploring the design
rules for efficient membrane-reshaping nanostructures. Physical Review Letters.
125(22), 228101.
mla: Forster, Joel C., et al. “Exploring the Design Rules for Efficient Membrane-Reshaping
Nanostructures.” Physical Review Letters, vol. 125, no. 22, 228101, American
Physical Society, 2020, doi:10.1103/physrevlett.125.228101.
short: J.C. Forster, J. Krausser, M.R. Vuyyuru, B. Baum, A. Šarić, Physical Review
Letters 125 (2020).
date_created: 2021-11-26T07:10:43Z
date_published: 2020-11-23T00:00:00Z
date_updated: 2024-10-16T12:59:57Z
day: '23'
ddc:
- '530'
doi: 10.1103/physrevlett.125.228101
extern: '1'
external_id:
pmid:
- '33315453'
file:
- access_level: open_access
checksum: fbf2e1415e332d6add90222d60401a1d
content_type: application/pdf
creator: cchlebak
date_created: 2021-11-26T07:16:49Z
date_updated: 2021-11-26T07:16:49Z
file_id: '10345'
file_name: 2020_PhysRevLett_Forster.pdf
file_size: 844353
relation: main_file
success: 1
file_date_updated: 2021-11-26T07:16:49Z
has_accepted_license: '1'
intvolume: ' 125'
issue: '22'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://www.biorxiv.org/content/10.1101/2020.02.27.968149v1
month: '11'
oa: 1
oa_version: Published Version
pmid: 1
publication: Physical Review Letters
publication_identifier:
eissn:
- 1079-7114
issn:
- 0031-9007
publication_status: published
publisher: American Physical Society
quality_controlled: '1'
scopus_import: '1'
status: public
title: Exploring the design rules for efficient membrane-reshaping nanostructures
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 0043cee0-e5fc-11ee-9736-f83bc23afbf0
volume: 125
year: '2020'
...
---
OA_place: publisher
OA_type: hybrid
_id: '10346'
abstract:
- lang: eng
text: One of the most robust examples of self-assembly in living organisms is the
formation of collagen architectures. Collagen type I molecules are a crucial component
of the extracellular matrix, where they self-assemble into fibrils of well-defined
axial striped patterns. This striped fibrillar pattern is preserved across the
animal kingdom and is important for the determination of cell phenotype, cell
adhesion, and tissue regulation and signaling. The understanding of the physical
processes that determine such a robust morphology of self-assembled collagen fibrils
is currently almost completely missing. Here, we develop a minimal coarse-grained
computational model to identify the physical principles of the assembly of collagen-mimetic
molecules. We find that screened electrostatic interactions can drive the formation
of collagen-like filaments of well-defined striped morphologies. The fibril axial
pattern is determined solely by the distribution of charges on the molecule and
is robust to the changes in protein concentration, monomer rigidity, and environmental
conditions. We show that the striped fibrillar pattern cannot be easily predicted
from the interactions between two monomers but is an emergent result of multibody
interactions. Our results can help address collagen remodeling in diseases and
aging and guide the design of collagen scaffolds for biotechnological applications.
acknowledgement: We thank Melinda Duer, Patrick Mesquida, Lucy Colwell, Lucie Liu,
Daan Frenkel, and Ivan Palaia for helpful discussions. We acknowledge support from
the Engineering and Physical Sciences Research Council (A.E.H., L.K.D., and A.Š.),
Biotechnology and Biological Sciences Research Council LIDo programme (N.G.G. and
C.A.B.), the Royal Society (A.Š.), and the UK Materials and Molecular Modelling
Hub for computational resources, which is partially funded by EPSRC ( EP/P020194/1).
article_processing_charge: No
article_type: original
author:
- first_name: Anne E.
full_name: Hafner, Anne E.
last_name: Hafner
- first_name: Noemi G.
full_name: Gyori, Noemi G.
last_name: Gyori
- first_name: Ciaran A.
full_name: Bench, Ciaran A.
last_name: Bench
- first_name: Luke K.
full_name: Davis, Luke K.
last_name: Davis
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
citation:
ama: Hafner AE, Gyori NG, Bench CA, Davis LK, Šarić A. Modeling fibrillogenesis
of collagen-mimetic molecules. Biophysical Journal. 2020;119(9):1791-1799.
doi:10.1016/j.bpj.2020.09.013
apa: Hafner, A. E., Gyori, N. G., Bench, C. A., Davis, L. K., & Šarić, A. (2020).
Modeling fibrillogenesis of collagen-mimetic molecules. Biophysical Journal.
Cell Press. https://doi.org/10.1016/j.bpj.2020.09.013
chicago: Hafner, Anne E., Noemi G. Gyori, Ciaran A. Bench, Luke K. Davis, and Anđela
Šarić. “Modeling Fibrillogenesis of Collagen-Mimetic Molecules.” Biophysical
Journal. Cell Press, 2020. https://doi.org/10.1016/j.bpj.2020.09.013.
ieee: A. E. Hafner, N. G. Gyori, C. A. Bench, L. K. Davis, and A. Šarić, “Modeling
fibrillogenesis of collagen-mimetic molecules,” Biophysical Journal, vol.
119, no. 9. Cell Press, pp. 1791–1799, 2020.
ista: Hafner AE, Gyori NG, Bench CA, Davis LK, Šarić A. 2020. Modeling fibrillogenesis
of collagen-mimetic molecules. Biophysical Journal. 119(9), 1791–1799.
mla: Hafner, Anne E., et al. “Modeling Fibrillogenesis of Collagen-Mimetic Molecules.”
Biophysical Journal, vol. 119, no. 9, Cell Press, 2020, pp. 1791–99, doi:10.1016/j.bpj.2020.09.013.
short: A.E. Hafner, N.G. Gyori, C.A. Bench, L.K. Davis, A. Šarić, Biophysical Journal
119 (2020) 1791–1799.
date_created: 2021-11-26T07:27:24Z
date_published: 2020-09-23T00:00:00Z
date_updated: 2024-10-16T13:05:34Z
day: '23'
doi: 10.1016/j.bpj.2020.09.013
extern: '1'
external_id:
pmid:
- '33049216'
intvolume: ' 119'
issue: '9'
keyword:
- biophysics
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://www.biorxiv.org/content/10.1101/2020.06.08.140061v1
month: '09'
oa: 1
oa_version: Published Version
page: 1791-1799
pmid: 1
publication: Biophysical Journal
publication_identifier:
issn:
- 0006-3495
publication_status: published
publisher: Cell Press
quality_controlled: '1'
scopus_import: '1'
status: public
title: Modeling fibrillogenesis of collagen-mimetic molecules
type: journal_article
user_id: 0043cee0-e5fc-11ee-9736-f83bc23afbf0
volume: 119
year: '2020'
...
---
_id: '10347'
abstract:
- lang: eng
text: Understanding the mechanism of action of compounds capable of inhibiting amyloid-fibril
formation is critical to the development of potential therapeutics against protein-misfolding
diseases. A fundamental challenge for progress is the range of possible target
species and the disparate timescales involved, since the aggregating proteins
are simultaneously the reactants, products, intermediates, and catalysts of the
reaction. It is a complex problem, therefore, to choose the states of the aggregating
proteins that should be bound by the compounds to achieve the most potent inhibition.
We present here a comprehensive kinetic theory of amyloid-aggregation inhibition
that reveals the fundamental thermodynamic and kinetic signatures characterizing
effective inhibitors by identifying quantitative relationships between the aggregation
and binding rate constants. These results provide general physical laws to guide
the design and optimization of inhibitors of amyloid-fibril formation, revealing
in particular the important role of on-rates in the binding of the inhibitors.
acknowledgement: We acknowledge support from Peterhouse, Cambridge (T.C.T.M.); the
Swiss National Science Foundation (T.C.T.M.); the Royal Society (A.S. and S.C.);
the Academy of Medical Sciences (A.S.); Sidney Sussex College, Cambridge (G.M.);
Newnham College, Cambridge (G.T.H.); the Wellcome Trust (T.P.J.K.); the Cambridge
Center for Misfolding Diseases (T.P.J.K. and M.V.); the Biotechnology and Biological
Sciences Research Council (T.P.J.K.); the Frances and Augustus Newman Foundation
(T.P.J.K.); and the Synapsis Foundation for Alzheimer’s disease (P.A.). The research
leading to these results has received funding from the European Research Council
(ERC) under the European Union’s Seventh Framework Program (FP7/2007-2013) through
the ERC Grant PhysProt (Agreement 337969).
article_processing_charge: No
article_type: original
author:
- first_name: Thomas C. T.
full_name: Michaels, Thomas C. T.
last_name: Michaels
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Georg
full_name: Meisl, Georg
last_name: Meisl
- first_name: Gabriella T.
full_name: Heller, Gabriella T.
last_name: Heller
- first_name: Samo
full_name: Curk, Samo
last_name: Curk
- first_name: Paolo
full_name: Arosio, Paolo
last_name: Arosio
- first_name: Sara
full_name: Linse, Sara
last_name: Linse
- first_name: Christopher M.
full_name: Dobson, Christopher M.
last_name: Dobson
- first_name: Michele
full_name: Vendruscolo, Michele
last_name: Vendruscolo
- first_name: Tuomas P. J.
full_name: Knowles, Tuomas P. J.
last_name: Knowles
citation:
ama: Michaels TCT, Šarić A, Meisl G, et al. Thermodynamic and kinetic design principles
for amyloid-aggregation inhibitors. Proceedings of the National Academy of
Sciences. 2020;117(39):24251-24257. doi:10.1073/pnas.2006684117
apa: Michaels, T. C. T., Šarić, A., Meisl, G., Heller, G. T., Curk, S., Arosio,
P., … Knowles, T. P. J. (2020). Thermodynamic and kinetic design principles for
amyloid-aggregation inhibitors. Proceedings of the National Academy of Sciences.
National Academy of Sciences. https://doi.org/10.1073/pnas.2006684117
chicago: Michaels, Thomas C. T., Anđela Šarić, Georg Meisl, Gabriella T. Heller,
Samo Curk, Paolo Arosio, Sara Linse, Christopher M. Dobson, Michele Vendruscolo,
and Tuomas P. J. Knowles. “Thermodynamic and Kinetic Design Principles for Amyloid-Aggregation
Inhibitors.” Proceedings of the National Academy of Sciences. National
Academy of Sciences, 2020. https://doi.org/10.1073/pnas.2006684117.
ieee: T. C. T. Michaels et al., “Thermodynamic and kinetic design principles
for amyloid-aggregation inhibitors,” Proceedings of the National Academy of
Sciences, vol. 117, no. 39. National Academy of Sciences, pp. 24251–24257,
2020.
ista: Michaels TCT, Šarić A, Meisl G, Heller GT, Curk S, Arosio P, Linse S, Dobson
CM, Vendruscolo M, Knowles TPJ. 2020. Thermodynamic and kinetic design principles
for amyloid-aggregation inhibitors. Proceedings of the National Academy of Sciences.
117(39), 24251–24257.
mla: Michaels, Thomas C. T., et al. “Thermodynamic and Kinetic Design Principles
for Amyloid-Aggregation Inhibitors.” Proceedings of the National Academy of
Sciences, vol. 117, no. 39, National Academy of Sciences, 2020, pp. 24251–57,
doi:10.1073/pnas.2006684117.
short: T.C.T. Michaels, A. Šarić, G. Meisl, G.T. Heller, S. Curk, P. Arosio, S.
Linse, C.M. Dobson, M. Vendruscolo, T.P.J. Knowles, Proceedings of the National
Academy of Sciences 117 (2020) 24251–24257.
date_created: 2021-11-26T07:48:27Z
date_published: 2020-09-14T00:00:00Z
date_updated: 2021-11-26T08:59:06Z
day: '14'
doi: 10.1073/pnas.2006684117
extern: '1'
external_id:
pmid:
- '32929030'
intvolume: ' 117'
issue: '39'
keyword:
- multidisciplinary
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://www.biorxiv.org/content/10.1101/2020.02.22.960716
month: '09'
oa: 1
oa_version: Published Version
page: 24251-24257
pmid: 1
publication: Proceedings of the National Academy of Sciences
publication_identifier:
eissn:
- 1091-6490
issn:
- 0027-8424
publication_status: published
publisher: National Academy of Sciences
quality_controlled: '1'
scopus_import: '1'
status: public
title: Thermodynamic and kinetic design principles for amyloid-aggregation inhibitors
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 117
year: '2020'
...
---
_id: '10348'
abstract:
- lang: eng
text: The endosomal sorting complex required for transport-III (ESCRT-III) catalyzes
membrane fission from within membrane necks, a process that is essential for many
cellular functions, from cell division to lysosome degradation and autophagy.
How it breaks membranes, though, remains unknown. Here, we characterize a sequential
polymerization of ESCRT-III subunits that, driven by a recruitment cascade and
by continuous subunit-turnover powered by the ATPase Vps4, induces membrane deformation
and fission. During this process, the exchange of Vps24 for Did2 induces a tilt
in the polymer-membrane interface, which triggers transition from flat spiral
polymers to helical filament to drive the formation of membrane protrusions, and
ends with the formation of a highly constricted Did2-Ist1 co-polymer that we show
is competent to promote fission when bound on the inside of membrane necks. Overall,
our results suggest a mechanism of stepwise changes in ESCRT-III filament structure
and mechanical properties via exchange of the filament subunits to catalyze ESCRT-III
activity.
acknowledgement: The authors thank Nicolas Chiaruttini, Jean Gruenberg, and Lena Harker-Kirschneck
for careful correction of this manuscript and helpful discussions. The authors want
to thank the NCCR Chemical Biology for constant support during this project. A.R.
acknowledges funding from the Swiss National Fund for Research (31003A_130520, 31003A_149975,
and 31003A_173087) and the European Research Council Consolidator (311536). A.Š.
acknowledges the European Research Council (802960). B.B. thanks the BBSRC (BB/K009001/1)
and Wellcome Trust (203276/Z/16/Z) for support. J.M.v.F. acknowledges funding through
an EMBO Long-Term Fellowship (ALTF 1065-2015), the European Commission FP7 (Marie
Curie Actions, LTFCOFUND2013, and GA-2013-609409), and a Transitional Postdoc fellowship
(2015/345) from the Swiss SystemsX.ch initiative, evaluated by the Swiss National
Science Foundation and Swiss National Science Foundation Research (SNSF SINERGIA
160728/1 [leader, Sophie Martin]).
article_processing_charge: No
article_type: original
author:
- first_name: Anna-Katharina
full_name: Pfitzner, Anna-Katharina
last_name: Pfitzner
- first_name: Vincent
full_name: Mercier, Vincent
last_name: Mercier
- first_name: Xiuyun
full_name: Jiang, Xiuyun
last_name: Jiang
- first_name: Joachim
full_name: Moser von Filseck, Joachim
last_name: Moser von Filseck
- first_name: Buzz
full_name: Baum, Buzz
last_name: Baum
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Aurélien
full_name: Roux, Aurélien
last_name: Roux
citation:
ama: Pfitzner A-K, Mercier V, Jiang X, et al. An ESCRT-III polymerization sequence
drives membrane deformation and fission. Cell. 2020;182(5):1140-1155.e18.
doi:10.1016/j.cell.2020.07.021
apa: Pfitzner, A.-K., Mercier, V., Jiang, X., Moser von Filseck, J., Baum, B., Šarić,
A., & Roux, A. (2020). An ESCRT-III polymerization sequence drives membrane
deformation and fission. Cell. Elsevier. https://doi.org/10.1016/j.cell.2020.07.021
chicago: Pfitzner, Anna-Katharina, Vincent Mercier, Xiuyun Jiang, Joachim Moser
von Filseck, Buzz Baum, Anđela Šarić, and Aurélien Roux. “An ESCRT-III Polymerization
Sequence Drives Membrane Deformation and Fission.” Cell. Elsevier, 2020.
https://doi.org/10.1016/j.cell.2020.07.021.
ieee: A.-K. Pfitzner et al., “An ESCRT-III polymerization sequence drives
membrane deformation and fission,” Cell, vol. 182, no. 5. Elsevier, p.
1140–1155.e18, 2020.
ista: Pfitzner A-K, Mercier V, Jiang X, Moser von Filseck J, Baum B, Šarić A, Roux
A. 2020. An ESCRT-III polymerization sequence drives membrane deformation and
fission. Cell. 182(5), 1140–1155.e18.
mla: Pfitzner, Anna-Katharina, et al. “An ESCRT-III Polymerization Sequence Drives
Membrane Deformation and Fission.” Cell, vol. 182, no. 5, Elsevier, 2020,
p. 1140–1155.e18, doi:10.1016/j.cell.2020.07.021.
short: A.-K. Pfitzner, V. Mercier, X. Jiang, J. Moser von Filseck, B. Baum, A. Šarić,
A. Roux, Cell 182 (2020) 1140–1155.e18.
date_created: 2021-11-26T08:02:27Z
date_published: 2020-08-18T00:00:00Z
date_updated: 2021-11-26T08:58:37Z
day: '18'
doi: 10.1016/j.cell.2020.07.021
extern: '1'
external_id:
pmid:
- '32814015'
intvolume: ' 182'
issue: '5'
keyword:
- general biochemistry
- genetics and molecular biology
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://www.sciencedirect.com/science/article/pii/S0092867420309296
month: '08'
oa: 1
oa_version: Published Version
page: 1140-1155.e18
pmid: 1
publication: Cell
publication_identifier:
issn:
- 0092-8674
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: An ESCRT-III polymerization sequence drives membrane deformation and fission
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 182
year: '2020'
...
---
_id: '10349'
abstract:
- lang: eng
text: Sulfolobus acidocaldarius is the closest experimentally tractable archaeal
relative of eukaryotes and, despite lacking obvious cyclin-dependent kinase and
cyclin homologs, has an ordered eukaryote-like cell cycle with distinct phases
of DNA replication and division. Here, in exploring the mechanism of cell division
in S. acidocaldarius, we identify a role for the archaeal proteasome in regulating
the transition from the end of one cell cycle to the beginning of the next. Further,
we identify the archaeal ESCRT-III homolog, CdvB, as a key target of the proteasome
and show that its degradation triggers division by allowing constriction of the
CdvB1:CdvB2 ESCRT-III division ring. These findings offer a minimal mechanism
for ESCRT-III–mediated membrane remodeling and point to a conserved role for the
proteasome in eukaryotic and archaeal cell cycle control.
acknowledgement: "We thank the MRC LMCB at UCL for their support; the flow cytometry
STP at the Francis Crick Institute for assistance, with special thanks to S. Purewal
and D. Davis; C. Bertoli for mentorship\r\nand advice; J. M. Garcia-Arcos for help
early on in this project; the entire Baum lab for their input throughout the project;
the Albers lab for advice and reagents, with special thanks to M. Van Wolferen and
S. Albers; the members of the Wellcome consortium for archaeal cytoskeleton studies
for advice and comments; and J. Löwe, S. Oliferenko, M. Balasubramanian, and D.
Gerlich for discussions and advice on the manuscript. N.P.R. and S.B. would like
to thank N. Rzechorzek, A. Simon, and S. Anjum for discussion and advice."
article_processing_charge: No
article_type: original
author:
- first_name: Gabriel
full_name: Tarrason Risa, Gabriel
last_name: Tarrason Risa
- first_name: Fredrik
full_name: Hurtig, Fredrik
last_name: Hurtig
- first_name: Sian
full_name: Bray, Sian
last_name: Bray
- first_name: Anne E.
full_name: Hafner, Anne E.
last_name: Hafner
- first_name: Lena
full_name: Harker-Kirschneck, Lena
last_name: Harker-Kirschneck
- first_name: Peter
full_name: Faull, Peter
last_name: Faull
- first_name: Colin
full_name: Davis, Colin
last_name: Davis
- first_name: Dimitra
full_name: Papatziamou, Dimitra
last_name: Papatziamou
- first_name: Delyan R.
full_name: Mutavchiev, Delyan R.
last_name: Mutavchiev
- first_name: Catherine
full_name: Fan, Catherine
last_name: Fan
- first_name: Leticia
full_name: Meneguello, Leticia
last_name: Meneguello
- first_name: Andre
full_name: Arashiro Pulschen, Andre
last_name: Arashiro Pulschen
- first_name: Gautam
full_name: Dey, Gautam
last_name: Dey
- first_name: Siân
full_name: Culley, Siân
last_name: Culley
- first_name: Mairi
full_name: Kilkenny, Mairi
last_name: Kilkenny
- first_name: Diorge P.
full_name: Souza, Diorge P.
last_name: Souza
- first_name: Luca
full_name: Pellegrini, Luca
last_name: Pellegrini
- first_name: Robertus A. M.
full_name: de Bruin, Robertus A. M.
last_name: de Bruin
- first_name: Ricardo
full_name: Henriques, Ricardo
last_name: Henriques
- first_name: Ambrosius P.
full_name: Snijders, Ambrosius P.
last_name: Snijders
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Ann-Christin
full_name: Lindås, Ann-Christin
last_name: Lindås
- first_name: Nicholas P.
full_name: Robinson, Nicholas P.
last_name: Robinson
- first_name: Buzz
full_name: Baum, Buzz
last_name: Baum
citation:
ama: Tarrason Risa G, Hurtig F, Bray S, et al. The proteasome controls ESCRT-III–mediated
cell division in an archaeon. Science. 2020;369(6504). doi:10.1126/science.aaz2532
apa: Tarrason Risa, G., Hurtig, F., Bray, S., Hafner, A. E., Harker-Kirschneck,
L., Faull, P., … Baum, B. (2020). The proteasome controls ESCRT-III–mediated cell
division in an archaeon. Science. American Association for the Advancement
of Science. https://doi.org/10.1126/science.aaz2532
chicago: Tarrason Risa, Gabriel, Fredrik Hurtig, Sian Bray, Anne E. Hafner, Lena
Harker-Kirschneck, Peter Faull, Colin Davis, et al. “The Proteasome Controls ESCRT-III–Mediated
Cell Division in an Archaeon.” Science. American Association for the Advancement
of Science, 2020. https://doi.org/10.1126/science.aaz2532.
ieee: G. Tarrason Risa et al., “The proteasome controls ESCRT-III–mediated
cell division in an archaeon,” Science, vol. 369, no. 6504. American Association
for the Advancement of Science, 2020.
ista: Tarrason Risa G, Hurtig F, Bray S, Hafner AE, Harker-Kirschneck L, Faull P,
Davis C, Papatziamou D, Mutavchiev DR, Fan C, Meneguello L, Arashiro Pulschen
A, Dey G, Culley S, Kilkenny M, Souza DP, Pellegrini L, de Bruin RAM, Henriques
R, Snijders AP, Šarić A, Lindås A-C, Robinson NP, Baum B. 2020. The proteasome
controls ESCRT-III–mediated cell division in an archaeon. Science. 369(6504).
mla: Tarrason Risa, Gabriel, et al. “The Proteasome Controls ESCRT-III–Mediated
Cell Division in an Archaeon.” Science, vol. 369, no. 6504, American Association
for the Advancement of Science, 2020, doi:10.1126/science.aaz2532.
short: G. Tarrason Risa, F. Hurtig, S. Bray, A.E. Hafner, L. Harker-Kirschneck,
P. Faull, C. Davis, D. Papatziamou, D.R. Mutavchiev, C. Fan, L. Meneguello, A.
Arashiro Pulschen, G. Dey, S. Culley, M. Kilkenny, D.P. Souza, L. Pellegrini,
R.A.M. de Bruin, R. Henriques, A.P. Snijders, A. Šarić, A.-C. Lindås, N.P. Robinson,
B. Baum, Science 369 (2020).
date_created: 2021-11-26T08:21:34Z
date_published: 2020-08-07T00:00:00Z
date_updated: 2021-11-26T08:58:33Z
day: '07'
doi: 10.1126/science.aaz2532
extern: '1'
external_id:
pmid:
- '32764038'
intvolume: ' 369'
issue: '6504'
keyword:
- multidisciplinary
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://www.biorxiv.org/content/10.1101/774273v1
month: '08'
oa: 1
oa_version: Preprint
pmid: 1
publication: Science
publication_identifier:
eissn:
- 1095-9203
issn:
- 0036-8075
publication_status: published
publisher: American Association for the Advancement of Science
quality_controlled: '1'
scopus_import: '1'
status: public
title: The proteasome controls ESCRT-III–mediated cell division in an archaeon
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 369
year: '2020'
...
---
_id: '10350'
abstract:
- lang: eng
text: The misfolding and aberrant aggregation of proteins into fibrillar structures
is a key factor in some of the most prevalent human diseases, including diabetes
and dementia. Low molecular weight oligomers are thought to be a central factor
in the pathology of these diseases, as well as critical intermediates in the fibril
formation process, and as such have received much recent attention. Moreover,
on-pathway oligomeric intermediates are potential targets for therapeutic strategies
aimed at interrupting the fibril formation process. However, a consistent framework
for distinguishing on-pathway from off-pathway oligomers has hitherto been lacking
and, in particular, no consensus definition of on- and off-pathway oligomers is
available. In this paper, we argue that a non-binary definition of oligomers'
contribution to fibril-forming pathways may be more informative and we suggest
a quantitative framework, in which each oligomeric species is assigned a value
between 0 and 1 describing its relative contribution to the formation of fibrils.
First, we clarify the distinction between oligomers and fibrils, and then we use
the formalism of reaction networks to develop a general definition for on-pathway
oligomers, that yields meaningful classifications in the context of amyloid formation.
By applying these concepts to Monte Carlo simulations of a minimal aggregating
system, and by revisiting several previous studies of amyloid oligomers in light
of our new framework, we demonstrate how to perform these classifications in practice.
For each oligomeric species we obtain the degree to which it is on-pathway, highlighting
the most effective pharmaceutical targets for the inhibition of amyloid fibril
formation.
acknowledgement: We are grateful to the Schiff Foundation (AJD), Peterhouse, Cambridge
(TCTM), the Swiss National Science foundation (TCTM), Ramon Jenkins Fellowship,
Sidney Sussex, Cambridge (GM), the Royal Society (AŠ), the Academy of Medical Sciences
and Wellcome Trust (AŠ), the Danish Research Council (MK), the Lundbeck Foundation
(MK), the Swedish Research Council (SL), the Wellcome Trust (TPJK), the Cambridge
Centre for Misfolding Diseases (TPJK), the BBSRC (TPJK), the Frances and Augustus
Newman Foundation (TPJK) for financial support. The research leading to these results
has received funding from the European Research Council under the European Union's
Seventh Framework Programme (FP7/2007-2013) through the ERC grants PhysProt (agreement
no. 337969), MAMBA (agreement no. 340890) and NovoNordiskFonden (SL).
article_processing_charge: No
article_type: original
author:
- first_name: Alexander J.
full_name: Dear, Alexander J.
last_name: Dear
- first_name: Georg
full_name: Meisl, Georg
last_name: Meisl
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Thomas C. T.
full_name: Michaels, Thomas C. T.
last_name: Michaels
- first_name: Magnus
full_name: Kjaergaard, Magnus
last_name: Kjaergaard
- first_name: Sara
full_name: Linse, Sara
last_name: Linse
- first_name: Tuomas P. J.
full_name: Knowles, Tuomas P. J.
last_name: Knowles
citation:
ama: Dear AJ, Meisl G, Šarić A, et al. Identification of on- and off-pathway oligomers
in amyloid fibril formation. Chemical Science. 2020;11(24):6236-6247. doi:10.1039/c9sc06501f
apa: Dear, A. J., Meisl, G., Šarić, A., Michaels, T. C. T., Kjaergaard, M., Linse,
S., & Knowles, T. P. J. (2020). Identification of on- and off-pathway oligomers
in amyloid fibril formation. Chemical Science. Royal Society of Chemistry.
https://doi.org/10.1039/c9sc06501f
chicago: Dear, Alexander J., Georg Meisl, Anđela Šarić, Thomas C. T. Michaels, Magnus
Kjaergaard, Sara Linse, and Tuomas P. J. Knowles. “Identification of On- and off-Pathway
Oligomers in Amyloid Fibril Formation.” Chemical Science. Royal Society
of Chemistry, 2020. https://doi.org/10.1039/c9sc06501f.
ieee: A. J. Dear et al., “Identification of on- and off-pathway oligomers
in amyloid fibril formation,” Chemical Science, vol. 11, no. 24. Royal
Society of Chemistry, pp. 6236–6247, 2020.
ista: Dear AJ, Meisl G, Šarić A, Michaels TCT, Kjaergaard M, Linse S, Knowles TPJ.
2020. Identification of on- and off-pathway oligomers in amyloid fibril formation.
Chemical Science. 11(24), 6236–6247.
mla: Dear, Alexander J., et al. “Identification of On- and off-Pathway Oligomers
in Amyloid Fibril Formation.” Chemical Science, vol. 11, no. 24, Royal
Society of Chemistry, 2020, pp. 6236–47, doi:10.1039/c9sc06501f.
short: A.J. Dear, G. Meisl, A. Šarić, T.C.T. Michaels, M. Kjaergaard, S. Linse,
T.P.J. Knowles, Chemical Science 11 (2020) 6236–6247.
date_created: 2021-11-26T09:08:19Z
date_published: 2020-06-08T00:00:00Z
date_updated: 2021-11-26T11:21:20Z
day: '08'
doi: 10.1039/c9sc06501f
extern: '1'
external_id:
pmid:
- '32953019'
intvolume: ' 11'
issue: '24'
keyword:
- general chemistry
language:
- iso: eng
license: https://creativecommons.org/licenses/by-nc/3.0/
main_file_link:
- open_access: '1'
url: https://pubs.rsc.org/en/content/articlehtml/2020/sc/c9sc06501f
month: '06'
oa: 1
oa_version: Published Version
page: 6236-6247
pmid: 1
publication: Chemical Science
publication_identifier:
eissn:
- 2041-6539
issn:
- 2041-6520
publication_status: published
publisher: Royal Society of Chemistry
quality_controlled: '1'
scopus_import: '1'
status: public
title: Identification of on- and off-pathway oligomers in amyloid fibril formation
tmp:
image: /images/cc_by_nc.png
legal_code_url: https://creativecommons.org/licenses/by-nc/3.0/legalcode
name: Creative Commons Attribution-NonCommercial 3.0 Unported (CC BY-NC 3.0)
short: CC BY-NC (3.0)
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 11
year: '2020'
...
---
_id: '10351'
abstract:
- lang: eng
text: Oligomeric species populated during the aggregation of the Aβ42 peptide have
been identified as potent cytotoxins linked to Alzheimer’s disease, but the fundamental
molecular pathways that control their dynamics have yet to be elucidated. By developing
a general approach that combines theory, experiment and simulation, we reveal,
in molecular detail, the mechanisms of Aβ42 oligomer dynamics during amyloid fibril
formation. Even though all mature amyloid fibrils must originate as oligomers,
we found that most Aβ42 oligomers dissociate into their monomeric precursors without
forming new fibrils. Only a minority of oligomers converts into fibrillar structures.
Moreover, the heterogeneous ensemble of oligomeric species interconverts on timescales
comparable to those of aggregation. Our results identify fundamentally new steps
that could be targeted by therapeutic interventions designed to combat protein
misfolding diseases.
acknowledgement: We acknowledge support from Peterhouse (T.C.T.M.), the Swiss National
Science foundation (T.C.T.M.), the Royal Society (A.Š.), the Academy of Medical
Sciences (A.Š.), the UCL Institute for the Physics of Living Systems (S.C.), Sidney
Sussex College (G.M.), the Wellcome Trust (A.Š., M.V., C.M.D. and T.P.J.K.), the
Schiff Foundation (A.J.D.), the Cambridge Centre for Misfolding Diseases (M.V.,
C.M.D. and T.P.J.K.), the BBSRC (C.M.D. and T.P.J.K.), the Frances and Augustus
Newman Foundation (T.P.J.K.), the Swedish Research Council (S.L.) and the ERC grant
MAMBA (S.L., agreement no. 340890). The research that led to these results received
funding from the European Research Council under the European Union’s Seventh Framework
Programme (FP7/2007-2013) through the ERC grant PhysProt (agreement no. 337969).
article_processing_charge: No
article_type: original
author:
- first_name: Thomas C. T.
full_name: Michaels, Thomas C. T.
last_name: Michaels
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Samo
full_name: Curk, Samo
last_name: Curk
- first_name: Katja
full_name: Bernfur, Katja
last_name: Bernfur
- first_name: Paolo
full_name: Arosio, Paolo
last_name: Arosio
- first_name: Georg
full_name: Meisl, Georg
last_name: Meisl
- first_name: Alexander J.
full_name: Dear, Alexander J.
last_name: Dear
- first_name: Samuel I. A.
full_name: Cohen, Samuel I. A.
last_name: Cohen
- first_name: Christopher M.
full_name: Dobson, Christopher M.
last_name: Dobson
- first_name: Michele
full_name: Vendruscolo, Michele
last_name: Vendruscolo
- first_name: Sara
full_name: Linse, Sara
last_name: Linse
- first_name: Tuomas P. J.
full_name: Knowles, Tuomas P. J.
last_name: Knowles
citation:
ama: Michaels TCT, Šarić A, Curk S, et al. Dynamics of oligomer populations formed
during the aggregation of Alzheimer’s Aβ42 peptide. Nature Chemistry. 2020;12(5):445-451.
doi:10.1038/s41557-020-0452-1
apa: Michaels, T. C. T., Šarić, A., Curk, S., Bernfur, K., Arosio, P., Meisl, G.,
… Knowles, T. P. J. (2020). Dynamics of oligomer populations formed during the
aggregation of Alzheimer’s Aβ42 peptide. Nature Chemistry. Springer Nature.
https://doi.org/10.1038/s41557-020-0452-1
chicago: Michaels, Thomas C. T., Anđela Šarić, Samo Curk, Katja Bernfur, Paolo Arosio,
Georg Meisl, Alexander J. Dear, et al. “Dynamics of Oligomer Populations Formed
during the Aggregation of Alzheimer’s Aβ42 Peptide.” Nature Chemistry.
Springer Nature, 2020. https://doi.org/10.1038/s41557-020-0452-1.
ieee: T. C. T. Michaels et al., “Dynamics of oligomer populations formed
during the aggregation of Alzheimer’s Aβ42 peptide,” Nature Chemistry,
vol. 12, no. 5. Springer Nature, pp. 445–451, 2020.
ista: Michaels TCT, Šarić A, Curk S, Bernfur K, Arosio P, Meisl G, Dear AJ, Cohen
SIA, Dobson CM, Vendruscolo M, Linse S, Knowles TPJ. 2020. Dynamics of oligomer
populations formed during the aggregation of Alzheimer’s Aβ42 peptide. Nature
Chemistry. 12(5), 445–451.
mla: Michaels, Thomas C. T., et al. “Dynamics of Oligomer Populations Formed during
the Aggregation of Alzheimer’s Aβ42 Peptide.” Nature Chemistry, vol. 12,
no. 5, Springer Nature, 2020, pp. 445–51, doi:10.1038/s41557-020-0452-1.
short: T.C.T. Michaels, A. Šarić, S. Curk, K. Bernfur, P. Arosio, G. Meisl, A.J.
Dear, S.I.A. Cohen, C.M. Dobson, M. Vendruscolo, S. Linse, T.P.J. Knowles, Nature
Chemistry 12 (2020) 445–451.
date_created: 2021-11-26T09:15:13Z
date_published: 2020-04-13T00:00:00Z
date_updated: 2021-11-26T11:21:08Z
day: '13'
doi: 10.1038/s41557-020-0452-1
extern: '1'
external_id:
pmid:
- '32303714'
intvolume: ' 12'
issue: '5'
keyword:
- general chemical engineering
- general chemistry
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://www.biorxiv.org/content/10.1101/2020.01.08.897488
month: '04'
oa: 1
oa_version: None
page: 445-451
pmid: 1
publication: Nature Chemistry
publication_identifier:
eissn:
- 1755-4349
issn:
- 1755-4330
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
related_material:
link:
- relation: erratum
url: https://doi.org/10.1038/s41557-020-0468-6
scopus_import: '1'
status: public
title: Dynamics of oligomer populations formed during the aggregation of Alzheimer’s
Aβ42 peptide
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 12
year: '2020'
...
---
_id: '10352'
abstract:
- lang: eng
text: In the nuclear pore complex, intrinsically disordered nuclear pore proteins
(FG Nups) form a selective barrier for transport into and out of the cell nucleus,
in a way that remains poorly understood. The collective FG Nup behavior has long
been conceptualized either as a polymer brush, dominated by entropic and excluded-volume
(repulsive) interactions, or as a hydrogel, dominated by cohesive (attractive)
interactions between FG Nups. Here we compare mesoscale computational simulations
with a wide range of experimental data to demonstrate that FG Nups are at the
crossover point between these two regimes. Specifically, we find that repulsive
and attractive interactions are balanced, resulting in morphologies and dynamics
that are close to those of ideal polymer chains. We demonstrate that this property
of FG Nups yields sufficient cohesion to seal the transport barrier, and yet maintains
fast dynamics at the molecular scale, permitting the rapid polymer rearrangements
needed for transport events.
acknowledgement: We thank Dino Osmanović (MIT), Roy Beck (Tel-Aviv), Larissa Kapinos
(Basel), Roderick Lim (Basel), Ralf Richter (Leeds), and Anton Zilman (Toronto)
for discussions. This work was funded by the Royal Society (A.Š.) and the UK Engineering
and Physical Sciences Research Council (EP/L504889/1, B.W.H.).
article_number: '022420'
article_processing_charge: No
article_type: original
author:
- first_name: Luke K.
full_name: Davis, Luke K.
last_name: Davis
- first_name: Ian J.
full_name: Ford, Ian J.
last_name: Ford
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Bart W.
full_name: Hoogenboom, Bart W.
last_name: Hoogenboom
citation:
ama: Davis LK, Ford IJ, Šarić A, Hoogenboom BW. Intrinsically disordered nuclear
pore proteins show ideal-polymer morphologies and dynamics. Physical Review
E. 2020;101(2). doi:10.1103/physreve.101.022420
apa: Davis, L. K., Ford, I. J., Šarić, A., & Hoogenboom, B. W. (2020). Intrinsically
disordered nuclear pore proteins show ideal-polymer morphologies and dynamics.
Physical Review E. American Physical Society. https://doi.org/10.1103/physreve.101.022420
chicago: Davis, Luke K., Ian J. Ford, Anđela Šarić, and Bart W. Hoogenboom. “Intrinsically
Disordered Nuclear Pore Proteins Show Ideal-Polymer Morphologies and Dynamics.”
Physical Review E. American Physical Society, 2020. https://doi.org/10.1103/physreve.101.022420.
ieee: L. K. Davis, I. J. Ford, A. Šarić, and B. W. Hoogenboom, “Intrinsically disordered
nuclear pore proteins show ideal-polymer morphologies and dynamics,” Physical
Review E, vol. 101, no. 2. American Physical Society, 2020.
ista: Davis LK, Ford IJ, Šarić A, Hoogenboom BW. 2020. Intrinsically disordered
nuclear pore proteins show ideal-polymer morphologies and dynamics. Physical Review
E. 101(2), 022420.
mla: Davis, Luke K., et al. “Intrinsically Disordered Nuclear Pore Proteins Show
Ideal-Polymer Morphologies and Dynamics.” Physical Review E, vol. 101,
no. 2, 022420, American Physical Society, 2020, doi:10.1103/physreve.101.022420.
short: L.K. Davis, I.J. Ford, A. Šarić, B.W. Hoogenboom, Physical Review E 101 (2020).
date_created: 2021-11-26T09:41:04Z
date_published: 2020-02-28T00:00:00Z
date_updated: 2021-11-26T11:21:16Z
day: '28'
doi: 10.1103/physreve.101.022420
extern: '1'
external_id:
pmid:
- '32168597'
intvolume: ' 101'
issue: '2'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://www.biorxiv.org/content/10.1101/571687
month: '02'
oa: 1
oa_version: Preprint
pmid: 1
publication: Physical Review E
publication_identifier:
eissn:
- 2470-0053
issn:
- 2470-0045
publication_status: published
publisher: American Physical Society
quality_controlled: '1'
scopus_import: '1'
status: public
title: Intrinsically disordered nuclear pore proteins show ideal-polymer morphologies
and dynamics
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 101
year: '2020'
...
---
_id: '10353'
abstract:
- lang: eng
text: Experiments have suggested that bacterial mechanosensitive channels separate
into 2D clusters, the role of which is unclear. By developing a coarse-grained
computer model we find that clustering promotes the channel closure, which is
highly dependent on the channel concentration and membrane stress. This behaviour
yields a tightly regulated gating system, whereby at high tensions channels gate
individually, and at lower tensions the channels spontaneously aggregate and inactivate.
We implement this positive feedback into the model for cell volume regulation,
and find that the channel clustering protects the cell against excessive loss
of cytoplasmic content.
acknowledgement: We thank Samantha Miller, Bert Poolman, and the members of Šarić
and Pilizota laboratories for useful discussion. We acknowledge support from the
Engineering and Physical Sciences Research Council (A.P. and A.Š.), the UCL Institute
for the Physics of Living Systems (A.P. and A.Š.), Darwin Trust of University of
Edinburgh (H.S.), Industrial Biotechnology Innovation Centre (H.S. and T.P.), BBSRC
Council Crossing Biological Membrane Network (H.S. and T.P.), BBSRC/EPSRC/MRC Synthetic
Biology Research Centre (T.P.), and the Royal Society (A.Š.).
article_number: '048102'
article_processing_charge: No
article_type: original
author:
- first_name: Alexandru
full_name: Paraschiv, Alexandru
last_name: Paraschiv
- first_name: Smitha
full_name: Hegde, Smitha
last_name: Hegde
- first_name: Raman
full_name: Ganti, Raman
last_name: Ganti
- first_name: Teuta
full_name: Pilizota, Teuta
last_name: Pilizota
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
citation:
ama: Paraschiv A, Hegde S, Ganti R, Pilizota T, Šarić A. Dynamic clustering regulates
activity of mechanosensitive membrane channels. Physical Review Letters.
2020;124(4). doi:10.1103/physrevlett.124.048102
apa: Paraschiv, A., Hegde, S., Ganti, R., Pilizota, T., & Šarić, A. (2020).
Dynamic clustering regulates activity of mechanosensitive membrane channels. Physical
Review Letters. American Physical Society. https://doi.org/10.1103/physrevlett.124.048102
chicago: Paraschiv, Alexandru, Smitha Hegde, Raman Ganti, Teuta Pilizota, and Anđela
Šarić. “Dynamic Clustering Regulates Activity of Mechanosensitive Membrane Channels.”
Physical Review Letters. American Physical Society, 2020. https://doi.org/10.1103/physrevlett.124.048102.
ieee: A. Paraschiv, S. Hegde, R. Ganti, T. Pilizota, and A. Šarić, “Dynamic clustering
regulates activity of mechanosensitive membrane channels,” Physical Review
Letters, vol. 124, no. 4. American Physical Society, 2020.
ista: Paraschiv A, Hegde S, Ganti R, Pilizota T, Šarić A. 2020. Dynamic clustering
regulates activity of mechanosensitive membrane channels. Physical Review Letters.
124(4), 048102.
mla: Paraschiv, Alexandru, et al. “Dynamic Clustering Regulates Activity of Mechanosensitive
Membrane Channels.” Physical Review Letters, vol. 124, no. 4, 048102, American
Physical Society, 2020, doi:10.1103/physrevlett.124.048102.
short: A. Paraschiv, S. Hegde, R. Ganti, T. Pilizota, A. Šarić, Physical Review
Letters 124 (2020).
date_created: 2021-11-26T09:57:01Z
date_published: 2020-01-31T00:00:00Z
date_updated: 2021-11-26T11:21:12Z
day: '31'
doi: 10.1103/physrevlett.124.048102
extern: '1'
external_id:
pmid:
- '32058787'
intvolume: ' 124'
issue: '4'
keyword:
- general physics and astronomy
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://www.biorxiv.org/content/10.1101/553248
month: '01'
oa: 1
oa_version: Preprint
pmid: 1
publication: Physical Review Letters
publication_identifier:
eissn:
- 1079-7114
issn:
- 0031-9007
publication_status: published
publisher: American Physical Society
quality_controlled: '1'
scopus_import: '1'
status: public
title: Dynamic clustering regulates activity of mechanosensitive membrane channels
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 124
year: '2020'
...
---
OA_place: publisher
OA_type: hybrid
_id: '21083'
abstract:
- lang: eng
text: Helically folded aromatic oligoamide foldamers have a size and geometrical
parameters very distinct from those of α‐helices and are not obvious candidates
for α‐helix mimicry. Nevertheless, they offer multiple sites for attaching side
chains. It was found that some arrays of side chains at the surface of an aromatic
helix make it possible to mimic extended α‐helical surfaces. Synthetic methods
were developed to produce quinoline monomers suitably functionalized for solid
phase synthesis. A dodecamer was prepared. Its crystal structure validated the
initial design and showed helix bundling involving the α‐helix‐like interface.
These results open up new uses of aromatic helices to recognize protein surfaces
and to program helix bundling in water.
article_processing_charge: No
article_type: original
author:
- first_name: Márton
full_name: Zwillinger, Márton
last_name: Zwillinger
- first_name: Post Sai
full_name: Reddy, Post Sai
last_name: Reddy
- first_name: Barbara
full_name: Wicher, Barbara
last_name: Wicher
- first_name: Pradeep K
full_name: Mandal, Pradeep K
id: 6a3def15-d4b4-11ef-9fa9-a24c1f545ec3
last_name: Mandal
orcid: 0000-0001-5996-956X
- first_name: Márton
full_name: Csékei, Márton
last_name: Csékei
- first_name: Lucile
full_name: Fischer, Lucile
last_name: Fischer
- first_name: András
full_name: Kotschy, András
last_name: Kotschy
- first_name: Ivan
full_name: Huc, Ivan
last_name: Huc
citation:
ama: Zwillinger M, Reddy PS, Wicher B, et al. Aromatic foldamer helices as α‐helix
extended surface mimetics. Chemistry – A European Journal. 2020;26(72):17366-17370.
doi:10.1002/chem.202004064
apa: Zwillinger, M., Reddy, P. S., Wicher, B., Mandal, P. K., Csékei, M., Fischer,
L., … Huc, I. (2020). Aromatic foldamer helices as α‐helix extended surface mimetics.
Chemistry – A European Journal. Wiley. https://doi.org/10.1002/chem.202004064
chicago: Zwillinger, Márton, Post Sai Reddy, Barbara Wicher, Pradeep K Mandal, Márton
Csékei, Lucile Fischer, András Kotschy, and Ivan Huc. “Aromatic Foldamer Helices
as Α‐helix Extended Surface Mimetics.” Chemistry – A European Journal.
Wiley, 2020. https://doi.org/10.1002/chem.202004064.
ieee: M. Zwillinger et al., “Aromatic foldamer helices as α‐helix extended
surface mimetics,” Chemistry – A European Journal, vol. 26, no. 72. Wiley,
pp. 17366–17370, 2020.
ista: Zwillinger M, Reddy PS, Wicher B, Mandal PK, Csékei M, Fischer L, Kotschy
A, Huc I. 2020. Aromatic foldamer helices as α‐helix extended surface mimetics.
Chemistry – A European Journal. 26(72), 17366–17370.
mla: Zwillinger, Márton, et al. “Aromatic Foldamer Helices as Α‐helix Extended Surface
Mimetics.” Chemistry – A European Journal, vol. 26, no. 72, Wiley, 2020,
pp. 17366–70, doi:10.1002/chem.202004064.
short: M. Zwillinger, P.S. Reddy, B. Wicher, P.K. Mandal, M. Csékei, L. Fischer,
A. Kotschy, I. Huc, Chemistry – A European Journal 26 (2020) 17366–17370.
date_created: 2026-01-29T15:31:13Z
date_published: 2020-09-10T00:00:00Z
date_updated: 2026-02-20T06:53:53Z
day: '10'
ddc:
- '540'
doi: 10.1002/chem.202004064
extern: '1'
has_accepted_license: '1'
intvolume: ' 26'
issue: '72'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1002/chem.202004064
month: '09'
oa: 1
oa_version: Published Version
page: 17366-17370
publication: Chemistry – A European Journal
publication_identifier:
eissn:
- 1521-3765
issn:
- 0947-6539
publication_status: published
publisher: Wiley
quality_controlled: '1'
status: public
title: Aromatic foldamer helices as α‐helix extended surface mimetics
tmp:
image: /images/cc_by_nc.png
legal_code_url: https://creativecommons.org/licenses/by-nc/4.0/legalcode
name: Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)
short: CC BY-NC (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 26
year: '2020'
...
---
OA_place: repository
OA_type: green
_id: '21084'
abstract:
- lang: eng
text: Self-assembly is a powerful method to obtain large discrete functional molecular
architectures. When using a single building block, self-assembly generally yields
symmetrical objects in which all the subunits relate similarly to their neighbours.
Here we report the discovery of a family of self-constructing cyclic macromolecules
with stable folded conformations of low symmetry, which include some with a prime
number (13, 17 and 23) of units, despite being formed from a single component.
The formation of these objects amounts to the production of polymers with a perfectly
uniform length. Design rules for the spontaneous emergence of such macromolecules
include endowing monomers with a strong potential for non-covalent interactions
that remain frustrated in competing entropically favoured yet conformationally
restrained smaller cycles. The process can also be templated by a guest molecule
that itself has an asymmetrical structure, which paves the way to molecular imprinting
techniques at the level of single polymer chains.
article_processing_charge: No
article_type: original
author:
- first_name: Charalampos G.
full_name: Pappas, Charalampos G.
last_name: Pappas
- first_name: Pradeep K
full_name: Mandal, Pradeep K
id: 6a3def15-d4b4-11ef-9fa9-a24c1f545ec3
last_name: Mandal
orcid: 0000-0001-5996-956X
- first_name: Bin
full_name: Liu, Bin
last_name: Liu
- first_name: Brice
full_name: Kauffmann, Brice
last_name: Kauffmann
- first_name: Xiaoming
full_name: Miao, Xiaoming
last_name: Miao
- first_name: Dávid
full_name: Komáromy, Dávid
last_name: Komáromy
- first_name: Waldemar
full_name: Hoffmann, Waldemar
last_name: Hoffmann
- first_name: Christian
full_name: Manz, Christian
last_name: Manz
- first_name: Rayoon
full_name: Chang, Rayoon
last_name: Chang
- first_name: Kai
full_name: Liu, Kai
last_name: Liu
- first_name: Kevin
full_name: Pagel, Kevin
last_name: Pagel
- first_name: Ivan
full_name: Huc, Ivan
last_name: Huc
- first_name: Sijbren
full_name: Otto, Sijbren
last_name: Otto
citation:
ama: Pappas CG, Mandal PK, Liu B, et al. Emergence of low-symmetry foldamers from
single monomers. Nature Chemistry. 2020;12(12):1180-1186. doi:10.1038/s41557-020-00565-2
apa: Pappas, C. G., Mandal, P. K., Liu, B., Kauffmann, B., Miao, X., Komáromy, D.,
… Otto, S. (2020). Emergence of low-symmetry foldamers from single monomers. Nature
Chemistry. Springer Nature. https://doi.org/10.1038/s41557-020-00565-2
chicago: Pappas, Charalampos G., Pradeep K Mandal, Bin Liu, Brice Kauffmann, Xiaoming
Miao, Dávid Komáromy, Waldemar Hoffmann, et al. “Emergence of Low-Symmetry Foldamers
from Single Monomers.” Nature Chemistry. Springer Nature, 2020. https://doi.org/10.1038/s41557-020-00565-2.
ieee: C. G. Pappas et al., “Emergence of low-symmetry foldamers from single
monomers,” Nature Chemistry, vol. 12, no. 12. Springer Nature, pp. 1180–1186,
2020.
ista: Pappas CG, Mandal PK, Liu B, Kauffmann B, Miao X, Komáromy D, Hoffmann W,
Manz C, Chang R, Liu K, Pagel K, Huc I, Otto S. 2020. Emergence of low-symmetry
foldamers from single monomers. Nature Chemistry. 12(12), 1180–1186.
mla: Pappas, Charalampos G., et al. “Emergence of Low-Symmetry Foldamers from Single
Monomers.” Nature Chemistry, vol. 12, no. 12, Springer Nature, 2020, pp.
1180–86, doi:10.1038/s41557-020-00565-2.
short: C.G. Pappas, P.K. Mandal, B. Liu, B. Kauffmann, X. Miao, D. Komáromy, W.
Hoffmann, C. Manz, R. Chang, K. Liu, K. Pagel, I. Huc, S. Otto, Nature Chemistry
12 (2020) 1180–1186.
date_created: 2026-01-29T15:32:38Z
date_published: 2020-11-20T00:00:00Z
date_updated: 2026-02-23T11:46:11Z
day: '20'
doi: 10.1038/s41557-020-00565-2
extern: '1'
external_id:
pmid:
- '33219361 '
has_accepted_license: '1'
intvolume: ' 12'
issue: '12'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.26434/chemrxiv.10079186
month: '11'
oa: 1
oa_version: Preprint
page: 1180-1186
pmid: 1
publication: Nature Chemistry
publication_identifier:
eissn:
- 1755-4349
issn:
- 1755-4330
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
status: public
title: Emergence of low-symmetry foldamers from single monomers
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 12
year: '2020'
...
---
OA_place: publisher
OA_type: hybrid
_id: '21085'
abstract:
- lang: eng
text: Foldamers combining aliphatic and aromatic main-chain units often produce
atypical structures that cannot easily be accessed from purely aromatic or aliphatic
sequences. We report solid-state evidence that sequences comprising α-amino acids
and quinoline-based monomers adopt conformations that combine the folding propensities
of both components. Foldamers 2 and 3 having an XQQ repeat motif (X=α-amino acid,
Q=quinoline) were synthesized. Crystals of 2 (X=Phe, Q with an anionic side chain)
obtained from water revealed an aromatic helix where amide groups belonging to
the α-amino acids created a hydrogen-bond array typical of peptidic helices. Crystals
of 3 (X=Ser, Q with a lipophilic side chain) obtained from organic solvents revealed
a helix-turn-helix structure in which α-amino acid side chains interfere with
main-chain hydrogen bonding. High sequence-dependency of the conformation is typical
of peptides but is shown here to include aromatic folding features.
article_processing_charge: No
article_type: original
author:
- first_name: Xiaobo
full_name: Hu, Xiaobo
last_name: Hu
- first_name: Pradeep K
full_name: Mandal, Pradeep K
id: 6a3def15-d4b4-11ef-9fa9-a24c1f545ec3
last_name: Mandal
orcid: 0000-0001-5996-956X
- first_name: Brice
full_name: Kauffmann, Brice
last_name: Kauffmann
- first_name: Ivan
full_name: Huc, Ivan
last_name: Huc
citation:
ama: Hu X, Mandal PK, Kauffmann B, Huc I. Hybrid sequences that express both aromatic
amide and α‐peptidic folding features. ChemPlusChem. 2020;85(7):1580-1586.
doi:10.1002/cplu.202000416
apa: Hu, X., Mandal, P. K., Kauffmann, B., & Huc, I. (2020). Hybrid sequences
that express both aromatic amide and α‐peptidic folding features. ChemPlusChem.
Wiley. https://doi.org/10.1002/cplu.202000416
chicago: Hu, Xiaobo, Pradeep K Mandal, Brice Kauffmann, and Ivan Huc. “Hybrid Sequences
That Express Both Aromatic Amide and Α‐peptidic Folding Features.” ChemPlusChem.
Wiley, 2020. https://doi.org/10.1002/cplu.202000416.
ieee: X. Hu, P. K. Mandal, B. Kauffmann, and I. Huc, “Hybrid sequences that express
both aromatic amide and α‐peptidic folding features,” ChemPlusChem, vol.
85, no. 7. Wiley, pp. 1580–1586, 2020.
ista: Hu X, Mandal PK, Kauffmann B, Huc I. 2020. Hybrid sequences that express both
aromatic amide and α‐peptidic folding features. ChemPlusChem. 85(7), 1580–1586.
mla: Hu, Xiaobo, et al. “Hybrid Sequences That Express Both Aromatic Amide and Α‐peptidic
Folding Features.” ChemPlusChem, vol. 85, no. 7, Wiley, 2020, pp. 1580–86,
doi:10.1002/cplu.202000416.
short: X. Hu, P.K. Mandal, B. Kauffmann, I. Huc, ChemPlusChem 85 (2020) 1580–1586.
date_created: 2026-01-29T15:34:50Z
date_published: 2020-07-06T00:00:00Z
date_updated: 2026-02-20T06:51:31Z
day: '06'
doi: 10.1002/cplu.202000416
extern: '1'
external_id:
pmid:
- '32729681'
has_accepted_license: '1'
intvolume: ' 85'
issue: '7'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1002/cplu.202000416
month: '07'
oa: 1
oa_version: Published Version
page: 1580-1586
pmid: 1
publication: ChemPlusChem
publication_identifier:
eissn:
- 2192-6506
publication_status: published
publisher: Wiley
quality_controlled: '1'
scopus_import: '1'
status: public
title: Hybrid sequences that express both aromatic amide and α‐peptidic folding features
tmp:
image: /images/cc_by_nc.png
legal_code_url: https://creativecommons.org/licenses/by-nc/4.0/legalcode
name: Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)
short: CC BY-NC (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 85
year: '2020'
...
---
_id: '17444'
abstract:
- lang: eng
text: The first wafer-scale growth of site-controlled Ge/Si nanowires is reported
by Georgios Katsaros, Jian-Jun Zhang, and co-workers in article number 1906523.
They are highly uniform and their position, distance, length, and even square-
or L-shaped structures can all be precisely controlled. The electrically tunable
spin-orbit coupling demonstrated by transport measurements and the charge sensing
between quantum dots in closely spaced wires open a path toward scalable qubit
devices using nanowires on silicon.
article_number: '2070122'
article_processing_charge: No
author:
- first_name: Fei
full_name: Gao, Fei
last_name: Gao
- first_name: Jian‐Huan
full_name: Wang, Jian‐Huan
last_name: Wang
- first_name: Hannes
full_name: Watzinger, Hannes
id: 35DF8E50-F248-11E8-B48F-1D18A9856A87
last_name: Watzinger
- first_name: Hao
full_name: Hu, Hao
last_name: Hu
- first_name: Marko J.
full_name: Rančić, Marko J.
last_name: Rančić
- first_name: Jie‐Yin
full_name: Zhang, Jie‐Yin
last_name: Zhang
- first_name: Ting
full_name: Wang, Ting
last_name: Wang
- first_name: Yuan
full_name: Yao, Yuan
last_name: Yao
- first_name: Gui‐Lei
full_name: Wang, Gui‐Lei
last_name: Wang
- first_name: Josip
full_name: Kukucka, Josip
id: 3F5D8856-F248-11E8-B48F-1D18A9856A87
last_name: Kukucka
- first_name: Lada
full_name: Vukušić, Lada
id: 31E9F056-F248-11E8-B48F-1D18A9856A87
last_name: Vukušić
orcid: 0000-0003-2424-8636
- first_name: Christoph
full_name: Kloeffel, Christoph
last_name: Kloeffel
- first_name: Daniel
full_name: Loss, Daniel
last_name: Loss
- first_name: Feng
full_name: Liu, Feng
last_name: Liu
- first_name: Georgios
full_name: Katsaros, Georgios
id: 38DB5788-F248-11E8-B48F-1D18A9856A87
last_name: Katsaros
orcid: 0000-0001-8342-202X
- first_name: Jian‐Jun
full_name: Zhang, Jian‐Jun
last_name: Zhang
citation:
ama: 'Gao F, Wang J, Watzinger H, et al. Nanowires: Site‐controlled Uniform Ge/Si
Hut Wires with Electrically Tunable Spin–Orbit Coupling (Adv. Mater. 16/2020).
Vol 32. Wiley; 2020. doi:10.1002/adma.202070122'
apa: 'Gao, F., Wang, J., Watzinger, H., Hu, H., Rančić, M. J., Zhang, J., … Zhang,
J. (2020). Nanowires: Site‐controlled uniform Ge/Si Hut wires with electrically
tunable spin–orbit coupling (Adv. Mater. 16/2020). Advanced Materials
(Vol. 32). Wiley. https://doi.org/10.1002/adma.202070122'
chicago: 'Gao, Fei, Jian‐Huan Wang, Hannes Watzinger, Hao Hu, Marko J. Rančić, Jie‐Yin
Zhang, Ting Wang, et al. Nanowires: Site‐controlled Uniform Ge/Si Hut Wires
with Electrically Tunable Spin–Orbit Coupling (Adv. Mater. 16/2020). Advanced
Materials. Vol. 32. Wiley, 2020. https://doi.org/10.1002/adma.202070122.'
ieee: 'F. Gao et al., Nanowires: Site‐controlled uniform Ge/Si Hut wires
with electrically tunable spin–orbit coupling (Adv. Mater. 16/2020), vol.
32, no. 16. Wiley, 2020.'
ista: 'Gao F, Wang J, Watzinger H, Hu H, Rančić MJ, Zhang J, Wang T, Yao Y, Wang
G, Kukucka J, Vukušić L, Kloeffel C, Loss D, Liu F, Katsaros G, Zhang J. 2020.
Nanowires: Site‐controlled uniform Ge/Si Hut wires with electrically tunable spin–orbit
coupling (Adv. Mater. 16/2020), Wiley,p.'
mla: 'Gao, Fei, et al. “Nanowires: Site‐controlled Uniform Ge/Si Hut Wires with
Electrically Tunable Spin–Orbit Coupling (Adv. Mater. 16/2020).” Advanced Materials,
vol. 32, no. 16, 2070122, Wiley, 2020, doi:10.1002/adma.202070122.'
short: 'F. Gao, J. Wang, H. Watzinger, H. Hu, M.J. Rančić, J. Zhang, T. Wang, Y.
Yao, G. Wang, J. Kukucka, L. Vukušić, C. Kloeffel, D. Loss, F. Liu, G. Katsaros,
J. Zhang, Nanowires: Site‐controlled Uniform Ge/Si Hut Wires with Electrically
Tunable Spin–Orbit Coupling (Adv. Mater. 16/2020), Wiley, 2020.'
date_created: 2024-08-20T08:22:42Z
date_published: 2020-04-23T00:00:00Z
date_updated: 2025-06-12T07:16:21Z
day: '23'
department:
- _id: GeKa
doi: 10.1002/adma.202070122
intvolume: ' 32'
issue: '16'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1002/adma.202070122
month: '04'
oa: 1
oa_version: Published Version
publication: Advanced Materials
publication_identifier:
eissn:
- 1521-4095
issn:
- 0935-9648
publication_status: published
publisher: Wiley
quality_controlled: '1'
related_material:
record:
- id: '7541'
relation: other
status: public
status: public
title: 'Nanowires: Site‐controlled uniform Ge/Si Hut wires with electrically tunable
spin–orbit coupling (Adv. Mater. 16/2020)'
type: other_academic_publication
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 32
year: '2020'
...
---
_id: '17524'
abstract:
- lang: eng
text: The variability of quasars across multiple wavelengths is a useful probe of
physical conditions in active galactic nuclei. In particular, variable accretion
rates, instabilities, and reverberation effects in the accretion disc of a supermassive
black hole are expected to produce correlated flux variations in ultraviolet (UV)
and optical bands. Recent work has further argued that binary quasars should exhibit
strongly correlated UV and optical periodicities. Strong UV–optical correlations
have indeed been established in small samples of (N ≲ 30) quasars with well-sampled
light curves, and have extended the ‘bluer-when-brighter’ trend previously found
within the optical bands. Here, we further test the nature of quasar variability
by examining the observed-frame UV–optical correlations among bright quasars extracted
from the Half Million Quasars (HMQ) catalogue. We identified a large sample of
1315 quasars in HMQ with overlapping UV and optical light curves from the Galaxy
Evolution Explorer and the Catalina Real-time Transient Survey, respectively.
We find that strong correlations exist in this much larger sample, but we rule
out, at ∼95 per cent confidence, the simple hypothesis that the intrinsic UV and
optical variations of all quasars are fully correlated. Our results therefore
imply the existence of physical mechanism(s) that can generate uncorrelated optical
and UV flux variations.
article_processing_charge: No
article_type: original
author:
- first_name: Chengcheng
full_name: Xin, Chengcheng
last_name: Xin
- first_name: Maria
full_name: Charisi, Maria
last_name: Charisi
- first_name: Zoltán
full_name: Haiman, Zoltán
id: 7c006e8c-cc0d-11ee-8322-cb904ef76f36
last_name: Haiman
- first_name: David
full_name: Schiminovich, David
last_name: Schiminovich
citation:
ama: Xin C, Charisi M, Haiman Z, Schiminovich D. Correlation between optical and
UV variability of a large sample of quasars. Monthly Notices of the Royal Astronomical
Society. 2020;495(1):1403-1413. doi:10.1093/mnras/staa1258
apa: Xin, C., Charisi, M., Haiman, Z., & Schiminovich, D. (2020). Correlation
between optical and UV variability of a large sample of quasars. Monthly Notices
of the Royal Astronomical Society. Oxford University Press. https://doi.org/10.1093/mnras/staa1258
chicago: Xin, Chengcheng, Maria Charisi, Zoltán Haiman, and David Schiminovich.
“Correlation between Optical and UV Variability of a Large Sample of Quasars.”
Monthly Notices of the Royal Astronomical Society. Oxford University Press,
2020. https://doi.org/10.1093/mnras/staa1258.
ieee: C. Xin, M. Charisi, Z. Haiman, and D. Schiminovich, “Correlation between optical
and UV variability of a large sample of quasars,” Monthly Notices of the Royal
Astronomical Society, vol. 495, no. 1. Oxford University Press, pp. 1403–1413,
2020.
ista: Xin C, Charisi M, Haiman Z, Schiminovich D. 2020. Correlation between optical
and UV variability of a large sample of quasars. Monthly Notices of the Royal
Astronomical Society. 495(1), 1403–1413.
mla: Xin, Chengcheng, et al. “Correlation between Optical and UV Variability of
a Large Sample of Quasars.” Monthly Notices of the Royal Astronomical Society,
vol. 495, no. 1, Oxford University Press, 2020, pp. 1403–13, doi:10.1093/mnras/staa1258.
short: C. Xin, M. Charisi, Z. Haiman, D. Schiminovich, Monthly Notices of the Royal
Astronomical Society 495 (2020) 1403–1413.
date_created: 2024-09-05T09:27:32Z
date_published: 2020-05-07T00:00:00Z
date_updated: 2024-09-11T08:08:21Z
day: '07'
doi: 10.1093/mnras/staa1258
extern: '1'
intvolume: ' 495'
issue: '1'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1093/mnras/staa1258
month: '05'
oa: 1
oa_version: Published Version
page: 1403-1413
publication: Monthly Notices of the Royal Astronomical Society
publication_identifier:
issn:
- 0035-8711
- 1365-2966
publication_status: published
publisher: Oxford University Press
quality_controlled: '1'
scopus_import: '1'
status: public
title: Correlation between optical and UV variability of a large sample of quasars
type: journal_article
user_id: 317138e5-6ab7-11ef-aa6d-ffef3953e345
volume: 495
year: '2020'
...
---
_id: '17528'
abstract:
- lang: eng
text: 'We performed a series of numerical experiments to quantify the sensitivity
of the predictions for weak lensing statistics obtained in ray-tracing dark matter
(DM)-only simulations, to two hyper-parameters that influence the accuracy as
well as the computational cost of the predictions: the thickness of the lens planes
used to build past light cones and the mass resolution of the underlying DM simulation.
The statistics considered are the power spectrum (PS) and a series of non-Gaussian
observables, including the one-point probability density function, lensing peaks,
and Minkowski functionals. Counterintuitively, we find that using thin lens planes
(< 60 h−1 Mpc on a 240 h−1 Mpc simulation box) suppresses the PS over a broad
range of scales beyond what would be acceptable for a survey comparable to the
Large Synoptic Survey Telescope (LSST). A mass resolution of 7.2 × 1011 h−1 M⊙
per DM particle (or 2563 particles in a (240 h−1 Mpc)3 box) is sufficient to extract
information using the PS and non-Gaussian statistics from weak lensing data at
angular scales down to 1'' with LSST-like levels of shape noise.'
article_number: '284'
article_processing_charge: No
article_type: original
author:
- first_name: José Manuel Zorrilla
full_name: Matilla, José Manuel Zorrilla
last_name: Matilla
- first_name: Stefan
full_name: Waterval, Stefan
last_name: Waterval
- first_name: Zoltán
full_name: Haiman, Zoltán
id: 7c006e8c-cc0d-11ee-8322-cb904ef76f36
last_name: Haiman
citation:
ama: Matilla JMZ, Waterval S, Haiman Z. Optimizing simulation parameters for weak
lensing analyses involving non-Gaussian observables. The Astronomical Journal.
2020;159(6). doi:10.3847/1538-3881/ab8f8c
apa: Matilla, J. M. Z., Waterval, S., & Haiman, Z. (2020). Optimizing simulation
parameters for weak lensing analyses involving non-Gaussian observables. The
Astronomical Journal. American Astronomical Society. https://doi.org/10.3847/1538-3881/ab8f8c
chicago: Matilla, José Manuel Zorrilla, Stefan Waterval, and Zoltán Haiman. “Optimizing
Simulation Parameters for Weak Lensing Analyses Involving Non-Gaussian Observables.”
The Astronomical Journal. American Astronomical Society, 2020. https://doi.org/10.3847/1538-3881/ab8f8c.
ieee: J. M. Z. Matilla, S. Waterval, and Z. Haiman, “Optimizing simulation parameters
for weak lensing analyses involving non-Gaussian observables,” The Astronomical
Journal, vol. 159, no. 6. American Astronomical Society, 2020.
ista: Matilla JMZ, Waterval S, Haiman Z. 2020. Optimizing simulation parameters
for weak lensing analyses involving non-Gaussian observables. The Astronomical
Journal. 159(6), 284.
mla: Matilla, José Manuel Zorrilla, et al. “Optimizing Simulation Parameters for
Weak Lensing Analyses Involving Non-Gaussian Observables.” The Astronomical
Journal, vol. 159, no. 6, 284, American Astronomical Society, 2020, doi:10.3847/1538-3881/ab8f8c.
short: J.M.Z. Matilla, S. Waterval, Z. Haiman, The Astronomical Journal 159 (2020).
date_created: 2024-09-05T09:35:49Z
date_published: 2020-05-29T00:00:00Z
date_updated: 2024-09-11T09:03:15Z
day: '29'
doi: 10.3847/1538-3881/ab8f8c
extern: '1'
intvolume: ' 159'
issue: '6'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.3847/1538-3881/ab8f8c
month: '05'
oa: 1
oa_version: Published Version
publication: The Astronomical Journal
publication_identifier:
issn:
- 0004-6256
- 1538-3881
publication_status: published
publisher: American Astronomical Society
quality_controlled: '1'
scopus_import: '1'
status: public
title: Optimizing simulation parameters for weak lensing analyses involving non-Gaussian
observables
type: journal_article
user_id: 317138e5-6ab7-11ef-aa6d-ffef3953e345
volume: 159
year: '2020'
...
---
_id: '17529'
abstract:
- lang: eng
text: The astrophysical origin of gravitational wave (GW) events is one of the most
timely problems in the wake of the LIGO/Virgo discoveries. In active galactic
nuclei (AGN), binaries form and evolve efficiently by dynamical interactions and
gaseous dissipation. Previous studies have suggested that binary black hole (BBH)
mergers in AGN disks can contribute significantly to BBH mergers observed by GW
interferometers. Here we examine the distribution of the effective spin parameter
χeff of this GW source population. We extend our semi-analytical model of binary
formation and evolution in AGN disks by following the evolution of the binary
orbital angular momenta and black hole (BH) spins. BH spins change due to gas
accretion and BH mergers, while the binary orbital angular momenta evolve due
to gas accretion and binary-single interactions. We find that the distribution
of χeff predicted by our AGN model is similar to the distribution observed during
LIGO/Virgo O1 and O2. On the other hand, if radial migration of BHs is inefficient,
χeff is skewed toward higher values compared with the observed distribution, because
of the paucity of scattering events that would randomize spin directions relative
to the orbital plane. We suggest that high binary masses and the positive correlation
between binary mass and the standard deviation of χeff for chirp masses up to
≈20 M⊙, can be possible signatures for mergers originating in AGN disks. Finally,
hierarchical mergers in AGN disks naturally produce properties of the recent GW
event GW190412, including a low mass ratio, a high primary BH spin, and a significant
spin component in the orbital plane.
article_number: '26'
article_processing_charge: No
article_type: original
author:
- first_name: Hiromichi
full_name: Tagawa, Hiromichi
last_name: Tagawa
- first_name: Zoltán
full_name: Haiman, Zoltán
id: 7c006e8c-cc0d-11ee-8322-cb904ef76f36
last_name: Haiman
- first_name: Imre
full_name: Bartos, Imre
last_name: Bartos
- first_name: Bence
full_name: Kocsis, Bence
last_name: Kocsis
citation:
ama: Tagawa H, Haiman Z, Bartos I, Kocsis B. Spin evolution of stellar-mass black
hole binaries in active galactic nuclei. The Astrophysical Journal. 2020;899(1).
doi:10.3847/1538-4357/aba2cc
apa: Tagawa, H., Haiman, Z., Bartos, I., & Kocsis, B. (2020). Spin evolution
of stellar-mass black hole binaries in active galactic nuclei. The Astrophysical
Journal. American Astronomical Society. https://doi.org/10.3847/1538-4357/aba2cc
chicago: Tagawa, Hiromichi, Zoltán Haiman, Imre Bartos, and Bence Kocsis. “Spin
Evolution of Stellar-Mass Black Hole Binaries in Active Galactic Nuclei.” The
Astrophysical Journal. American Astronomical Society, 2020. https://doi.org/10.3847/1538-4357/aba2cc.
ieee: H. Tagawa, Z. Haiman, I. Bartos, and B. Kocsis, “Spin evolution of stellar-mass
black hole binaries in active galactic nuclei,” The Astrophysical Journal,
vol. 899, no. 1. American Astronomical Society, 2020.
ista: Tagawa H, Haiman Z, Bartos I, Kocsis B. 2020. Spin evolution of stellar-mass
black hole binaries in active galactic nuclei. The Astrophysical Journal. 899(1),
26.
mla: Tagawa, Hiromichi, et al. “Spin Evolution of Stellar-Mass Black Hole Binaries
in Active Galactic Nuclei.” The Astrophysical Journal, vol. 899, no. 1,
26, American Astronomical Society, 2020, doi:10.3847/1538-4357/aba2cc.
short: H. Tagawa, Z. Haiman, I. Bartos, B. Kocsis, The Astrophysical Journal 899
(2020).
date_created: 2024-09-05T09:36:37Z
date_published: 2020-08-10T00:00:00Z
date_updated: 2024-09-11T09:11:55Z
day: '10'
doi: 10.3847/1538-4357/aba2cc
extern: '1'
intvolume: ' 899'
issue: '1'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.3847/1538-4357/aba2cc
month: '08'
oa: 1
oa_version: Published Version
publication: The Astrophysical Journal
publication_identifier:
issn:
- 0004-637X
- 1538-4357
publication_status: published
publisher: American Astronomical Society
quality_controlled: '1'
scopus_import: '1'
status: public
title: Spin evolution of stellar-mass black hole binaries in active galactic nuclei
type: journal_article
user_id: 317138e5-6ab7-11ef-aa6d-ffef3953e345
volume: 899
year: '2020'
...
---
_id: '17537'
abstract:
- lang: eng
text: The recent gravitational wave merger event, GW190521, has challenged our understanding
of the stellar-mass black hole (BH) formation. The primary and secondary BH are
both inferred to fall inside the pair-instability (PI) mass gap. Here we propose
that the formation of such binaries is possible through gas accretion onto the
BH remnants of Population III (Pop~III) stars born in high-redshift (z>10) minihalos.
Once the parent halo has grown to the atomic-cooling limit, even brief episodes
of gas accretion in the dense central regions of the halo can increase the masses
of Pop~III remnant BHs above the PI limit. Starting with a BBH with an initial
mass of O(100) M⊙ we find that it would only need to spend about 100~Myr in the
inner few pc of an atomic-cooling halo to accrete about 50~M⊙ of material and
resemble a system similar to GW190521. The dynamical friction timescale for the
binary to sink to the dense inner region of its parent halo is comparable or shorter
than the accretion timescale required to increase their mass above the PI limit.
Once in the core of the halo, the binary can enter a phase of hyper-Eddington
accretion, where it would only take a few thousand years to exceed the PI limit
through accretion. Even more massive BBHs could form through this channel, and
be detectable by detectors with improved low-frequency sensitivity. Single Pop~III
BH remnants would also grow through accretion and could later form binaries dynamically.
As little as a few percent of Pop~III BH remnants may be sufficient to match the
rate of massive BBH mergers inferred from GW190521 of 0.13+0.3−0.11Gpc−3yr−1.
article_number: L21
article_processing_charge: No
article_type: original
author:
- first_name: Mohammadtaher
full_name: Safarzadeh, Mohammadtaher
last_name: Safarzadeh
- first_name: Zoltán
full_name: Haiman, Zoltán
id: 7c006e8c-cc0d-11ee-8322-cb904ef76f36
last_name: Haiman
citation:
ama: Safarzadeh M, Haiman Z. Formation of GW190521 via gas accretion onto population
III stellar black hole remnants born in high-redshift minihalos. The Astrophysical
Journal Letters. 2020;903(1). doi:10.3847/2041-8213/abc253
apa: Safarzadeh, M., & Haiman, Z. (2020). Formation of GW190521 via gas accretion
onto population III stellar black hole remnants born in high-redshift minihalos.
The Astrophysical Journal Letters. American Astronomical Society. https://doi.org/10.3847/2041-8213/abc253
chicago: Safarzadeh, Mohammadtaher, and Zoltán Haiman. “Formation of GW190521 via
Gas Accretion onto Population III Stellar Black Hole Remnants Born in High-Redshift
Minihalos.” The Astrophysical Journal Letters. American Astronomical Society,
2020. https://doi.org/10.3847/2041-8213/abc253.
ieee: M. Safarzadeh and Z. Haiman, “Formation of GW190521 via gas accretion onto
population III stellar black hole remnants born in high-redshift minihalos,” The
Astrophysical Journal Letters, vol. 903, no. 1. American Astronomical Society,
2020.
ista: Safarzadeh M, Haiman Z. 2020. Formation of GW190521 via gas accretion onto
population III stellar black hole remnants born in high-redshift minihalos. The
Astrophysical Journal Letters. 903(1), L21.
mla: Safarzadeh, Mohammadtaher, and Zoltán Haiman. “Formation of GW190521 via Gas
Accretion onto Population III Stellar Black Hole Remnants Born in High-Redshift
Minihalos.” The Astrophysical Journal Letters, vol. 903, no. 1, L21, American
Astronomical Society, 2020, doi:10.3847/2041-8213/abc253.
short: M. Safarzadeh, Z. Haiman, The Astrophysical Journal Letters 903 (2020).
date_created: 2024-09-05T09:50:29Z
date_published: 2020-11-02T00:00:00Z
date_updated: 2024-09-12T09:33:05Z
day: '02'
doi: 10.3847/2041-8213/abc253
extern: '1'
intvolume: ' 903'
issue: '1'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.3847/2041-8213/abc253
month: '11'
oa: 1
oa_version: Published Version
publication: The Astrophysical Journal Letters
publication_identifier:
issn:
- 2041-8205
- 2041-8213
publication_status: published
publisher: American Astronomical Society
quality_controlled: '1'
scopus_import: '1'
status: public
title: Formation of GW190521 via gas accretion onto population III stellar black hole
remnants born in high-redshift minihalos
type: journal_article
user_id: 317138e5-6ab7-11ef-aa6d-ffef3953e345
volume: 903
year: '2020'
...