From Fundamental Amyloid Protein Self-Assembly to Development of Bioplastics.

ABSTRACT: Proteins can self-assemble into a range of nanostructures as a result of molecular interactions. Amyloid nanofibrils, as one of them, were first discovered with regard to the relevance of neurodegenerative diseases but now have been exploited as building blocks to generate multiscale materials with designed functions for versatile applications. This review interconnects the mechanism of amyloid fibrillation, the current approaches to synthesizing amyloid protein-based materials, and the application in bioplastic development. We focus on the fundamental structures of self-assembled amyloid fibrils and how external factors can affect protein aggregation to optimize the process. Protein self-assembly is essentially the autonomous congregation of smaller protein units into larger, organized st

SUBMITTER: Li T 

PROVIDER: S-EPMC10777412 | biostudies-literature | 2024 Jan

REPOSITORIES: biostudies-literature