Gold‐Induced Fibril Growth: The Mechanism of Surface‐Facilitated Amyloid Aggregation

Abstract: The question of how amyloid fibril formation is influenced by surfaces is crucial for a detailed understanding of the process in vivo. We applied a combination of kinetic experiments and molecular dynamics simulations to elucidate how (model) surfaces influence fibril formation of the amyloid‐forming sequences of prion protein SUP35 and human islet amyloid polypeptide. The kinetic data suggest that structural reorganization of the initial peptide corona around colloidal gold nanoparticles is the rate‐limiting step. The molecular dynamics simulations reveal that partial physisorption to the surface results in the formation of aligned monolayers, which stimulate the formation of parallel, critical oligomers. The general mechanism implies that the competition between the underlying peptide–peptide and peptide–surface interactions must strike a balance to accelerate fibril formation.

Location
Deutsche Nationalbibliothek Frankfurt am Main
Extent
Online-Ressource
Language
Englisch

Bibliographic citation
Gold‐Induced Fibril Growth: The Mechanism of Surface‐Facilitated Amyloid Aggregation ; volume:55 ; number:37 ; year:2016 ; pages:11242-11246 ; extent:5
Angewandte Chemie / International edition. International edition ; 55, Heft 37 (2016), 11242-11246 (gesamt 5)

Creator
Gladytz, Anika
Abel, Bernd
Risselada, Herre Jelger

DOI
10.1002/anie.201605151
URN
urn:nbn:de:101:1-2022101107480421782869
Rights
Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
Last update
15.08.2025, 7:20 AM CEST

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Associated

  • Gladytz, Anika
  • Abel, Bernd
  • Risselada, Herre Jelger

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