Collagen Mimetic Peptides

Abstract

Since their first synthesis in the late 1960s, collagen mimetic peptides (CMPs) have been used as a molecular tool to study collagen, and as an approach to develop novel collagen mimetic biomaterials. Collagen, a major extracellular matrix (ECM) protein, plays vital roles in many physiological and pathogenic processes. Applications of CMPs have advanced our understanding of the structure and molecular properties of a collagen triple helix—the building block of collagen—and the interactions of collagen with important molecular ligands. The accumulating knowledge is also paving the way for developing novel CMPs for biomedical applications. Indeed, for the past 50 years, CMP research has been a fast-growing, far-reaching interdisciplinary field. The major development and achievement of CMPs were documented in a few detailed reviews around 2010. Here, we provided a brief overview of what we have learned about CMPs—their potential and their limitations. We focused on more recent developments in producing heterotrimeric CMPs, and CMPs that can form collagen-like higher order molecular assemblies. We also expanded the traditional view of CMPs to include larger designed peptides produced using recombinant systems. Studies using recombinant peptides have provided new insights on collagens and promoted progress in the development of collagen mimetic fibrillar self-assemblies.

Screening of Self-Assembling of Collagen IV Fragments into Stable Structures Potentially Useful in Regenerative Medicine

“…The uses of the CMP have made it possible to deepen the understanding of the structure and molecular properties of collagen triple helix and the interaction of collagen with molecular ligands. CMP has been used to create heterotrimeric CMP derivatives and CMP-based collagen-like materials [51].…”

The beauty of biocatalysis: sustainable synthesis of ingredients in cosmetics

“…Synthetic mimics of collagen have also been investigated, however due to the complexity of collagen there has been limited success. 306 That said, KOD is a synthetic mimic of collagen constructed from 36 amino acids. It self-assembles into triple-helix nanofibers and hydrogels and has shown to encourage desirable behaviour in platelets and whole blood plasma, therefore other functions may be possible and this opens doors to the use of other mimics in cosmetics.…”

Monomer‐scale design of functional protein polymers using consensus repeat sequences

“…We demonstrate that fundamental understanding of minimal consensus repeats drives the development of modular polymeric materials with well-defined sequences and functions. For other classes of highly repetitive proteins that also exhibit novel structural, mechanical, and thermal properties, we refer readers to extensive reviews of collagen-like proteins (repetitive (GXY) n domains, where X and Y enriched in proline and hydroxyproline) [64][65][66] and silklike proteins (alternating domains including but not limited to (A) n , (GA) n , (GGX) n , (GGXY n ). [67][68][69][70] These well-studied proteins have shorter repeat motifs clustered into larger domains, such that engineering domain sizes and ordering are more common than tuning monomer sequences to establish biopolymer structure-property relationships.…”