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- W2022687531 endingPage "141" @default.
- W2022687531 startingPage "131" @default.
- W2022687531 abstract "Collagen, a large insoluble protein with a characteristic triple helical structure, is found as the most prominent component of extracellular matrix. The functions of collagen are not limited to providing mechanical strength to various tissues and organs as a structural protein, as it has been pointed out that collagen exhibits various biological functions through specific interactions with other macromolecules. However, the use of native triple helical collagen is often troublesome because of its insolubility and gelating properties. Instead, triple helical collagen-like peptides have been designed and are used as collagen surrogates in studies on collagen structure, stability, and biological functions including binding to other proteins and cultured cells. This article reviews recent progress in peptide design, synthesis, and the applications of collagen-like peptides in current matrix biology, while emphasizing the advantages of the peptide-based strategy." @default.
- W2022687531 created "2016-06-24" @default.
- W2022687531 creator A5061696959 @default.
- W2022687531 date "2005-01-01" @default.
- W2022687531 modified "2023-10-17" @default.
- W2022687531 title "Triple Helical Collagen-Like Peptides: Engineering and Applications in Matrix Biology" @default.
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- W2022687531 doi "https://doi.org/10.1080/03008200591008518" @default.
- W2022687531 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/16147856" @default.
- W2022687531 hasPublicationYear "2005" @default.
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