Redesigned elastin domain-derived proteins inherit natural human elastin properties

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.

Statement of significance

Elastin, an essential protein in the human body, plays a crucial role in maintaining the functionality and structure of various connective tissues. Although elastin-like polypeptides (ELPs) exhibit desirable characteristics, their inability to fully encompass the intricacies of human elastin presents a notable limitation. In this study, we aimed to design elastin-like protein biomaterials that retain the favorable characteristics of human elastin while overcoming the limitations of natural and conventional ELPs. We believe that our study makes a significant contribution to the biomaterial field because we created three recombinant elastin domain-derived proteins (EDDPs) that overcome the limitations of the tropoelastin and ELP systems while maintaining essential elastin-like properties.