Collagen family proteins are the predominant components of extracellular matrices existing in all multicellular animals. They provide mechanical strength to tissues, and maintain structural integrity of organs. Also, collagens regulate various biological events, including cell attachment, migration, tissue regeneration and animal development. The specific functions of collagens are generally elicited by interactions of collagen-binding molecules (membrane receptors, soluble factors and other matrix components) with certain amino acid sequences displayed on the collagen triple helices. To date, numbers of functional sequences have been identified from the triple helical domains. Collagen is also acknowledged as one of useful biomaterials in regenerative medicine and tissue engineering. In this review, I summarize challenges made for the development of safer and highly-functional collagen surrogates by means of self-assembly of synthetic collagen-like peptides. I also describe other possible applications of collagen-like peptides in drug delivery focusing on the particular biophysical properties of the triple helical structure.
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