Structural stability and dynamics of an amyloid-forming peptide GNNQQNY from the yeast prion sup-35.

ABSTRACT: A seven amino acid yeast prion sup-35 fragment (GNNQQNY) forms amyloid fibrils. The availability of its detailed atomic oligomeric structure makes it a good model for studying the early stage of aggregation. Here we perform long all-atom explicit solvent molecular simulations of various sizes and arrangements of oligomer seeds of the wild-type and its mutants to study its stability and dynamics. Previous studies have suggested that the early stage rate-limiting step of oligomer formation occurs in high-order oligomers. Our simulations show that with the increase in the number of strands even from a dimer to a trimer, oligomer stability increases dramatically. This suggests that the minimal nucleus seed for GNNQQNY fibril formation could be small and is likely three or four peptides, in agr

SUBMITTER: Zheng J 

PROVIDER: S-EPMC1563778 | biostudies-literature | 2006 Aug

REPOSITORIES: biostudies-literature