Control of Nanoscale <i>In Situ</i> Protein Unfolding Defines Network Architecture and Mechanics of Protein Hydrogels.

ABSTRACT: Hierarchical assemblies of proteins exhibit a wide-range of material properties that are exploited both in nature and by artificially by humankind. However, little is understood about the importance of protein unfolding on the network assembly, severely limiting opportunities to utilize this nanoscale transition in the development of biomimetic and bioinspired materials. Here we control the force lability of a single protein building block, bovine serum albumin (BSA), and demonstrate that protein unfolding plays a critical role in defining the architecture and mechanics of a photochemically cross-linked native protein network. The internal nanoscale structure of BSA contains "molecular reinforcement" in the form of 17 covalent disulphide "nanostaples", preventing force-induced unfolding. U

SUBMITTER: Hughes MDG 

PROVIDER: S-EPMC8320229 | biostudies-literature | 2021 Jul

REPOSITORIES: biostudies-literature