Di-Tyrosine Cross-Linking of Elastin-Like Polypeptides through Ruthenium Photoreaction To Form Scaffolds: Fine Tuning Mechanical Properties and Improving Cytocompatibility.

Abstract

Ensuring that the mechanical properties of tissue engineering scaffolds align with those of the target tissues is crucial for their successful integration and functional performance. Tyrosine-tyrosine cross-links are found in nature in numerous proteins including resilin that exhibit enhanced toughness and energy storage capacity. Herein, we investigated the potential of tuning the mechanical properties of scaffolds made from elastin-like polypeptides (ELPs) containing tyrosine residues. Ruthenium-based photoreaction was used to form tyrosine cross-links. To enhance the cytocompatibility of the ELP scaffold, a continuous mode of washing was developed to remove residual ruthenium from the scaffolds. The continuous mode of washing was significantly superior in removing ruthenium and did so in a significantly shorter time as compared to batch washing and the conventional semibatch washing (also called dialysis washing). The range of storage moduli of the fabricated scaffolds spanned tens of Pa to hundreds of kPa. Human fibroblast cells were found to grow in the scaffolds and proliferate. Overall, this work offers a rationale for further developing tyrosine cross-linked ELPs for a broad range of tissue engineering applications.