Mechanism of Fibril and Soluble Oligomer Formation in Amyloid Beta and Hen Egg White Lysozyme Proteins.

ABSTRACT: Assembly and deposition of insoluble amyloid fibrils with a distinctive cross-β-sheet structure is the molecular hallmark of amyloidogenic diseases affecting the central nervous system as well as non-neuropathic amyloidosis. Amyloidogenic proteins form aggregates via kinetic pathways dictated by initial solution conditions. Often, early stage, cytotoxic, small globular amyloid oligomers (gOs) and curvilinear fibrils (CFs) precede the formation of late-stage rigid fibrils (RFs). Growing experimental evidence suggests that soluble gOs are off-pathway aggregates that do not directly convert into the final stage RFs. Yet, the kinetics of RFs aggregation under conditions that either promote or suppress the growth of gOs remain incompletely understood. Here we present a self-assembly model for a

SUBMITTER: Perez C 

PROVIDER: S-EPMC6839771 | biostudies-literature | 2019 Jul

REPOSITORIES: biostudies-literature