Designed triple-helical peptides as tools for collagen biochemistry and matrix engineering.
Collagens, characterized by a unique triple-helical structure, are the predominant component of extracellular matrices (ECMs) existing in all multicellular animals. Collagens not only maintain structural integrity of tissues and organs, but also regulate a number of biological events, including cell attachment, migration and differentiation, tissue regeneration and animal development. The specific functions of collagens are generally triggered by specific interactions of collagen-binding molecules (membrane receptors, soluble factors and other ECM components) with certain structures displayed on the collagen triple helices. Thus, synthetic triple-helical peptides that mimic the structure of native collagens have been used to investigate the individual collagen-protein interactions, as well as collagen structure and stability. The first part of this article illustrates the design of various collagen-mimetic peptides and their recent applications in matrix biology. Collagen is also acknowledged as one of the most promising biomaterials in regenerative medicine and tissue engineering. However, the use of animal-derived collagens in human could put the recipients at risks of pathogen transmission or allergic reactions. Hence, the production of safe artificial collagen surrogates is currently of considerable interest. The latter part of this article reviews recent attempts to develop artificial collagens as novel biomaterials.
Koide
Takaki
T
Faculty of Pharmaceutical Sciences, Niigata University of Pharmacy and Applied Life Sciences, Niigata 956-8603, Japan. koi@waseda.jp
D000818:Animals; D001672:Biocompatible Materials / Q000737:chemistry*; D003094:Collagen / Q000737:chemistry*; D005109:Extracellular Matrix / Q000737:chemistry*; D006801:Humans; D018716:Molecular Mimicry; D010455:Peptides / Q000737:chemistry*; D023822:Tissue Engineering
D001672:Biocompatible Materials; D010455:Peptides; D003094:Collagen