The browser you are using is not supported by this website. All versions of Internet Explorer are no longer supported, either by us or Microsoft (read more here: https://www.microsoft.com/en-us/microsoft-365/windows/end-of-ie-support).

Please use a modern browser to fully experience our website, such as the newest versions of Edge, Chrome, Firefox or Safari etc.

Spontaneous beta-barrel formation: an all-atom study of Abeta(16-22) oligomerization

På svenska

Author

Summary, in English

Using all-atom Monte Carlo simulations with implicit water, combined with a cluster size analysis, we study the aggregation of A16-22, a peptide capable of forming amyloid fibrils. We consider a system of six initially randomly oriented A16-22 peptides, and investigate the thermodynamics and structural properties of aggregates formed by this system. The system is unaggregated without ordered secondary structure at high temperature, and forms -sheet rich aggregates at low temperature. At the crossover between these two regimes, we find that clusters of all sizes occur, whereas the -strand content is low. In one of several runs, we observe the spontaneous formation of a -barrel with six antiparallel strands. The -barrel stands out as the by far most long-lived aggregate seen in our simulations.

Publishing year

2008

Language

English

Pages

207-214

Publication/Series

Proteins

Volume

71

Issue

1

Document type

Journal article

Publisher

John Wiley & Sons Inc.

Topic

  • Biophysics

Keywords

  • protein aggregation
  • self-assembly
  • cluster size analysis
  • amyloid-
  • protein misfolding

Status

Published

ISBN/ISSN/Other

  • ISSN: 0887-3585