Collagen, processed into several morphologies and originating from various sources, has long since been used as a biocompatible material that can assist wound healing and tissue regeneration. With the advent of biotechnology and solid-phase peptide synthesis, new possibilities arise to create rationally designed biomaterials based on collagen sequences incorporating new functionalities while maintaining the beneficial properties of natural collagen. In this study a new class of synthetic collagen materials is presented, defined by its simplistic core structure and its therefore predictable behavior. These so-called eCols (engineered collagens) consist of a varying number of Gly-Pro-Pro repeats, a redox-switchable aminoterminal nucleation site and an optional carboxyterminal cell adhesion motif. We show which of these proteins are able to self-assemble into triple helices and cross-linked gelatinous networks and provide insights into their cytocompatibility in vitro.
Keywords: biopolymer self-assembly; cell adhesion; collagen folding; synthetic peptides.