Conformational Variability of Amyloid-β and the Morphological Diversity of Its Aggregates.

ABSTRACT: Protein folding is the most fundamental and universal example of biomolecular self-organization and is characterized as an intramolecular process. In contrast, amyloidogenic proteins can interact with one another, leading to protein aggregation. The energy landscape of amyloid fibril formation is characterized by many minima for different competing low-energy structures and, therefore, is much more enigmatic than that of multiple folding pathways. Thus, to understand the entire energy landscape of protein aggregation, it is important to elucidate the full picture of conformational changes and polymorphisms of amyloidogenic proteins. This review provides an overview of the conformational diversity of amyloid-β (Aβ) characterized from experimental and theoretical approaches. Aβ exhibits a hi

SUBMITTER: Yagi-Utsumi M 

PROVIDER: S-EPMC9369837 | biostudies-literature | 2022 Jul

REPOSITORIES: biostudies-literature