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Anders Irbäck. Photo.

Anders Irbäck

Professor

Anders Irbäck. Photo.

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

Author

  • Anders Irbäck
  • Simon Mitternacht

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.

Department/s

  • Computational Biology and Biological Physics

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