β-barrel Oligomers as Common Intermediates of Peptides Self-Assembling into Cross-β Aggregates.

ABSTRACT: Oligomers populated during the early amyloid aggregation process are more toxic than mature fibrils, but pinpointing the exact toxic species among highly dynamic and heterogeneous aggregation intermediates remains a major challenge. β-barrel oligomers, structurally-determined recently for a slow-aggregating peptide derived from αB crystallin, are attractive candidates for exerting amyloid toxicity due to their well-defined structures as therapeutic targets and compatibility to the "amyloid-pore" hypothesis of toxicity. To assess whether β-barrel oligomers are common intermediates to amyloid peptides - a necessary step toward associating β-barrel oligomers with general amyloid cytotoxicity, we computationally studied the oligomerization and fibrillization dynamics of seven well-studied frag

SUBMITTER: Sun Y 

PROVIDER: S-EPMC6037789 | biostudies-literature | 2018 Jul

REPOSITORIES: biostudies-literature