A Comparison of the Mechanical Properties of ECM Components and Synthetic Self‐Assembling Peptides

Self-assembling peptide hydrogels are increasingly utilized in biomedical applications. The authors review the key mechanical properties of these structures across multiple size scales and compare them to that of native extracellular matrix components, which are found to display a much wider range of structural attributes. The authors then consider these findings in relation to cell response and future biomaterial design.

Abstract

The field of tissue engineering is increasingly moving away from a one-size-fits-all approach of simple synthetic homogeneous gels, and embracing more tailored designs to optimize cell function and differentiation for the organ of interest. Extracellular matrix (ECM) proteins are still the optimal route for controlling cell function, while a field of great promise is that of synthetic self-assembling peptides (SSAPs), which are fully biocompatible, biodegradable, and offer both the hierarchical structure and dynamic properties displayed by protein networks found in natural tissue. However, the mechanical properties of neither group have been comprehensively reviewed. In this review, rheological data and the Young's modulus of the most prevalent proteins involved in the ECM (collagen I, elastin, and fibronectin) are collated for the first time, and compared against the most widely researched SSAPs: peptide amphiphiles (PAs), β-sheets, β-hairpin peptides, and Fmoc-based gels (with a focus on PA-E3, RADA16, MAX1, and FmocFF, respectively).