---
res:
  bibo_abstract:
  - Primary nucleation is the fundamental event that initiates the conversion of proteins
    from their normal physiological forms into pathological amyloid aggregates associated
    with the onset and development of disorders including systemic amyloidosis, as
    well as the neurodegenerative conditions Alzheimer’s and Parkinson’s diseases.
    It has become apparent that the presence of surfaces can dramatically modulate
    nucleation. However, the underlying physicochemical parameters governing this
    process have been challenging to elucidate, with interfaces in some cases having
    been found to accelerate aggregation, while in others they can inhibit the kinetics
    of this process. Here we show through kinetic analysis that for three different
    fibril-forming proteins, interfaces affect the aggregation reaction mainly through
    modulating the primary nucleation step. Moreover, we show through direct measurements
    of the Gibbs free energy of adsorption, combined with theory and coarse-grained
    computer simulations, that overall nucleation rates are suppressed at high and
    at low surface interaction strengths but significantly enhanced at intermediate
    strengths, and we verify these regimes experimentally. Taken together, these results
    provide a quantitative description of the fundamental process which triggers amyloid
    formation and shed light on the key factors that control this process.@eng
  bibo_authorlist:
  - foaf_Person:
      foaf_givenName: Zenon
      foaf_name: Toprakcioglu, Zenon
      foaf_surname: Toprakcioglu
  - foaf_Person:
      foaf_givenName: Ayaka
      foaf_name: Kamada, Ayaka
      foaf_surname: Kamada
  - foaf_Person:
      foaf_givenName: Thomas C.T.
      foaf_name: Michaels, Thomas C.T.
      foaf_surname: Michaels
  - foaf_Person:
      foaf_givenName: Mengqi
      foaf_name: Xie, Mengqi
      foaf_surname: Xie
  - foaf_Person:
      foaf_givenName: Johannes
      foaf_name: Krausser, Johannes
      foaf_surname: Krausser
  - foaf_Person:
      foaf_givenName: Jiapeng
      foaf_name: Wei, Jiapeng
      foaf_surname: Wei
  - foaf_Person:
      foaf_givenName: Anđela
      foaf_name: Šarić, Anđela
      foaf_surname: Šarić
      foaf_workInfoHomepage: http://www.librecat.org/personId=bf63d406-f056-11eb-b41d-f263a6566d8b
    orcid: 0000-0002-7854-2139
  - foaf_Person:
      foaf_givenName: Michele
      foaf_name: Vendruscolo, Michele
      foaf_surname: Vendruscolo
  - foaf_Person:
      foaf_givenName: Tuomas P.J.
      foaf_name: Knowles, Tuomas P.J.
      foaf_surname: Knowles
  bibo_doi: 10.1073/pnas.2109718119
  bibo_issue: '31'
  bibo_volume: 119
  dct_date: 2022^xs_gYear
  dct_identifier:
  - UT:000903753500002
  dct_isPartOf:
  - http://id.crossref.org/issn/0027-8424
  - http://id.crossref.org/issn/1091-6490
  dct_language: eng
  dct_publisher: National Academy of Sciences@
  dct_title: Adsorption free energy predicts amyloid protein nucleation rates@
  fabio_hasPubmedId: '35901206'
...