Abstract

Elastin is distinguished by its exceptional elasticity and durability, resistance to degradation, prolonged lifespan, and ability to interact with cells. These favorable attributes have driven extensive research on elastin-like polypeptides (ELPs). Although ELPs exhibit desirable characteristics, their inability to fully encompass the intricacies of human elastin presents a notable limitation. Therefore, specifically engineered polypeptides have been designed using specific segments of human tropoelastin to create biocompatible elastin-like biomaterials suitable for tissue engineering. In this study, we redesigned and constructed three distinct types of elastin domain-derived proteins (EDDPs), each containing hydrophobic, cross-linking, and cellular interaction domains, with variations in the number of repeat domains within each polymer. Following the expression of recombinant EDDPs in a bacterial expression system, we investigated their mechanical properties, including the elastic modulus. The redesigned EDDPs exhibited favorable mechanical properties, biocompatibility, and cell-interaction capabilities, making them suitable as biomaterials. These findings highlight the potential of the redesigned EDDPs for various tissue engineering and regenerative medicine applications.

LINK: Redesigned elastin domain-derived proteins inherit natural human elastin properties - ScienceDirect

DOI: https://doi.org/10.1016/j.actbio.2025.07.071