Heterotrimeric collagen peptides: design, characterization, and applications

Abstract

Collagen is the most abundant protein in the human body. Over 90% of its total content is heterotrimers. Mutation of glycine in any polypeptide chain of natural heterotrimeric collagen will lead to genetic diseases. Due to the large molecular weight and complex structure of collagen, it is challenging to investigate collagen at the molecular level. Collagen peptides have been widely contributed to mimic collagen. Due to their small molecular weight and easily controlled structure, heterotrimeric collagen peptides can precisely mimic the chain composition, structure, and function of heterotrimeric collagen, such as type I and type IV collagen. This review describes in detail the design, characterization, and applications of heterotrimeric collagen peptides. Firstly, two strategies for constructing heterotrimeric collagen peptides have been summarized, involving covalent bonding and non-covalent interactions. Secondly, the methods for characterizing chain composition, triple helical structure, and thermal stability of heterotrimeric collagen peptides have been outlined. Furthermore, the application areas of heterotrimeric collagen peptides in simulating the chain registers and fibrous structure of collagen, as well as investigating the mechanisms of osteogenesis imperfecta, have been introduced. Finally, an outlook on the development of functionalized heterotrimeric collagen peptides and their potential applications in the field of biomedical research has been proposed.