---
_id: '18168'
abstract:
- lang: eng
text: 'Despite the considerable interest in the recombinant production of synthetic
spider silk fibers that possess mechanical properties similar to those of native
spider silks, such as the cost-effectiveness, tunability, and scalability realization,
is still lacking. To address this long-standing challenge, we have constructed
an artificial spider silk gene using Golden Gate assembly for the recombinant
bacterial production of dragline-mimicking silk, incorporating all the essential
components: the N-terminal domain, a 33-residue-long major-ampullate-spidroin-inspired
segment repeated 16 times, and the C-terminal domain (N16C). This designed silk-like
protein was successfully expressed in Escherichia coli, purified, and cast into
films from formic acid. We produced uniformly 13C–15N-labeled N16C films and employed
solid-state magic-angle spinning nuclear magnetic resonance (NMR) for characterization.
Thus, we could demonstrate that our bioengineered silk-like protein self-assembles
into a film where, when hydrated, the solvent-exposed layer of the rigid, β-nanocrystalline
polyalanine core undergoes a transition to an α-helical structure, gaining mobility
to the extent that it fully dissolves in water and transforms into a highly dynamic
random coil. This hydration-induced behavior induces chain dynamics in the glycine-rich
amorphous soft segments on the microsecond time scale, contributing to the elasticity
of the solid material. Our findings not only reveal the presence of structurally
and dynamically distinct segments within the film’s superstructure but also highlight
the complexity of the self-organization responsible for the exceptional mechanical
properties observed in proteins that mimic dragline silk.'
acknowledgement: We thank Dr. Pavel Kielkowski for performing the MS/MS measurement
and providing feedback on the manuscript. We are grateful to Rodrigo Ledesma Amaro
for introducing the Golden Gate Assembly technique in our lab. We acknowledge the
support from the Deutsche Forschungsgemeinschaft (DFG, German Research Foundation)─SFB
1309-325871075, the Center for NanoScience (CeNS), the Fonds der Chemischen Industrie,
and Universitätsgesellschaft München.
article_processing_charge: Yes (via OA deal)
article_type: original
author:
- first_name: Dongqing
full_name: Wu, Dongqing
last_name: Wu
- first_name: Anamaria
full_name: Koscic, Anamaria
last_name: Koscic
- first_name: Sonja
full_name: Schneider, Sonja
last_name: Schneider
- first_name: Romeo C. A.
full_name: Dubini, Romeo C. A.
last_name: Dubini
- first_name: Diana C.
full_name: Rodriguez Camargo, Diana C.
last_name: Rodriguez Camargo
- first_name: Sabine
full_name: Schneider, Sabine
last_name: Schneider
- first_name: Petra
full_name: Rovo, Petra
id: c316e53f-b965-11eb-b128-bb26acc59c00
last_name: Rovo
orcid: 0000-0001-8729-7326
citation:
ama: Wu D, Koscic A, Schneider S, et al. Unveiling the dynamic self-assembly of
a recombinant dragline-silk-mimicking protein. Biomacromolecules. 2024;25(3):1759-1774.
doi:10.1021/acs.biomac.3c01239
apa: Wu, D., Koscic, A., Schneider, S., Dubini, R. C. A., Rodriguez Camargo, D.
C., Schneider, S., & Rovo, P. (2024). Unveiling the dynamic self-assembly
of a recombinant dragline-silk-mimicking protein. Biomacromolecules. American
Chemical Society. https://doi.org/10.1021/acs.biomac.3c01239
chicago: Wu, Dongqing, Anamaria Koscic, Sonja Schneider, Romeo C. A. Dubini, Diana
C. Rodriguez Camargo, Sabine Schneider, and Petra Rovo. “Unveiling the Dynamic
Self-Assembly of a Recombinant Dragline-Silk-Mimicking Protein.” Biomacromolecules.
American Chemical Society, 2024. https://doi.org/10.1021/acs.biomac.3c01239.
ieee: D. Wu et al., “Unveiling the dynamic self-assembly of a recombinant
dragline-silk-mimicking protein,” Biomacromolecules, vol. 25, no. 3. American
Chemical Society, pp. 1759–1774, 2024.
ista: Wu D, Koscic A, Schneider S, Dubini RCA, Rodriguez Camargo DC, Schneider S,
Rovo P. 2024. Unveiling the dynamic self-assembly of a recombinant dragline-silk-mimicking
protein. Biomacromolecules. 25(3), 1759–1774.
mla: Wu, Dongqing, et al. “Unveiling the Dynamic Self-Assembly of a Recombinant
Dragline-Silk-Mimicking Protein.” Biomacromolecules, vol. 25, no. 3, American
Chemical Society, 2024, pp. 1759–74, doi:10.1021/acs.biomac.3c01239.
short: D. Wu, A. Koscic, S. Schneider, R.C.A. Dubini, D.C. Rodriguez Camargo, S.
Schneider, P. Rovo, Biomacromolecules 25 (2024) 1759–1774.
corr_author: '1'
date_created: 2024-10-02T10:09:53Z
date_published: 2024-03-11T00:00:00Z
date_updated: 2025-09-08T09:52:18Z
day: '11'
ddc:
- '540'
department:
- _id: NMR
doi: 10.1021/acs.biomac.3c01239
external_id:
isi:
- '001166501000001'
pmid:
- '38343096'
file:
- access_level: open_access
checksum: 9552b6d52f1e8a350764849a535fc13e
content_type: application/pdf
creator: dernst
date_created: 2024-10-07T08:33:35Z
date_updated: 2024-10-07T08:33:35Z
file_id: '18180'
file_name: 2024_BioMacromolecules_Wu.pdf
file_size: 6597227
relation: main_file
success: 1
file_date_updated: 2024-10-07T08:33:35Z
has_accepted_license: '1'
intvolume: ' 25'
isi: 1
issue: '3'
language:
- iso: eng
month: '03'
oa: 1
oa_version: Published Version
page: 1759-1774
pmid: 1
publication: Biomacromolecules
publication_identifier:
eissn:
- 1526-4602
issn:
- 1525-7797
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
scopus_import: '1'
status: public
title: Unveiling the dynamic self-assembly of a recombinant dragline-silk-mimicking
protein
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: 317138e5-6ab7-11ef-aa6d-ffef3953e345
volume: 25
year: '2024'
...