Secondary Structures and Mechanical Properties of Biomimetic Protein Polymers

Silk may possess superior mechanical strength while its resilience is very poor. In contrast, elastin in human arteries is very soft but extremely durable with an estimated half-life of 70 years. By combing polypeptide sequences derived from native silk and elastin, we have produced a series of silk-elastin-like proteins (SELPs), which have displayed a set of outstanding properties such as good biocompatibility and controllable biodegradation rates [1]. In this study, we will examine the crystallization of the silk-like blocks and the crosslinking of the elastin-like blocks, as well as their influences on the mechanical behavior of SELPs. The ultimate goal of this study is to explore the potential of SELPs for applications in the engineering of load-bearing tissues such as arteries.