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

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.

• Författare: Anders Irbäck; Simon Mitternacht
• Avdelning/ar: Beräkningsbiologi och biologisk fysik - Har omorganiserats
• Publiceringsår: 2008
• Språk: Engelska
• Sidor: 207-214
• Publikation/Tidskrift/Serie: Proteins
• Volym: 71
• Issue: 1
• Länkar: http://dx.doi.org/10.1002/prot.21682
• Dokumenttyp: Artikel i tidskrift
• Förlag: John Wiley & Sons Inc.
• Ämne: Biophysics
• Nyckelord: protein aggregation; self-assembly; cluster size analysis; amyloid-; protein misfolding
• Status: Published
• ISBN/ISSN/Övrigt: ISSN: 0887-3585