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• W2055695196 abstract "Recent widespread interest in the development of engineered tissue and organ replacement therapies has prompted demand for new approaches to immobilize exogenous components to natural collagen. Chemical coupling of synthetic moieties to amino acid side chains has been commonly practiced for such purposes; however, such coupling reactions are difficult to control on large proteins and are generally not conducive to modifying integrated collagen scaffolds that contain live cells and tissues. As an alternative to the conventional covalent modification method, we have developed a novel physical modification technique that is based on collagen's native ability to associate into a triple-helical molecular architecture. Here, we present a finding that collagen mimetic peptides (CMPs) of sequence -(Pro-Hyp-Gly)x- exhibit strong affinity to both native and gelatinized type I collagen under controlled thermal conditions. We also show that the cell adhesion characteristics of collagen can be readily altered by applying a poly(ethylene glycol)-CMP conjugate to a prefabricated collagen film." @default.
• W2055695196 created "2016-06-24" @default.
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• W2055695196 date "2005-03-01" @default.
• W2055695196 modified "2023-10-17" @default.
• W2055695196 title "Facile Modification of Collagen Directed by Collagen Mimetic Peptides" @default.
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• W2055695196 doi "https://doi.org/10.1021/ja0431915" @default.
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