Order-Disorder Balance in Silk-Elastin-like Polypeptides Determines Their Self-Assembly into Hydrogel Networks.

ABSTRACT: The biofabrication of recombinant structural proteins with a range of mechanical or structural features usually relies on the generation of protein libraries displaying variations in terms of amino acid composition, block structure, molecular weight, or physical/chemical cross-linking sites. This approach, while highly successful in generating a wealth of knowledge regarding the links between design features and material properties, has some inherent limitations related to its low throughput. This slows down the pace of the development of de novo recombinant structural proteins. Here, we propose an approach to tune the viscoelastic properties of temperature-responsive hydrogels made of silk-elastin-like polypeptides (SELPs) without modifying their sequence. To do so, we subject puri

SUBMITTER: Lopez Barreiro D 

PROVIDER: S-EPMC11783522 | biostudies-literature | 2025 Jan

REPOSITORIES: biostudies-literature