
Anders Irbäck
Professor

Spontaneous beta-barrel formation: an all-atom study of Abeta(16-22) oligomerization
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.
Department/s
- Computational Biology and Biological Physics - Undergoing reorganization
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