Multistep Changes in Amyloid Structure Induced by Cross-Seeding on a Rugged Energy Landscape.

ABSTRACT: Amyloid fibrils are aberrant protein aggregates associated with various amyloidoses and neurodegenerative diseases. It is recently indicated that structural diversity of amyloid fibrils often results in different pathological phenotypes, including cytotoxicity and infectivity. The diverse structures are predicted to propagate by seed-dependent growth, which is one of the characteristic properties of amyloid fibrils. However, much remains unknown regarding how exactly the amyloid structures are inherited to subsequent generations by seeding reaction. Here, we investigated the behaviors of self- and cross-seeding of amyloid fibrils of human and bovine insulin in terms of thioflavin T fluorescence, morphology, secondary structure, and iodine staining. Insulin amyloid fibrils exhibited differe

SUBMITTER: Yuzu K 

PROVIDER: S-EPMC7840402 | biostudies-literature | 2021 Jan

REPOSITORIES: biostudies-literature