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Stabilization of collagen-model, triple-helical peptides for in vitro and in vivo applications.

ABSTRACT: The triple-helical structure of collagen has been accurately reproduced in numerous chemical and recombinant model systems. Triple-helical peptides and proteins have found application for dissecting collagen-stabilizing forces, isolating receptor- and protein-binding sites in collagen, mechanistic examination of collagenolytic proteases, and development of novel biomaterials. Introduction of native-like sequences into triple-helical constructs can reduce the thermal stability of the triple-helix to below that of the physiological environment. In turn, incorporation of nonnative amino acids and/or templates can enhance triple-helix stability. We presently describe approaches by which triple-helical structure can be modulated for use under physiological or near-physiological conditions.

SUBMITTER: Bhowmick M

PROVIDER: S-EPMC4260935 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature

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Stabilization of collagen-model, triple-helical peptides for in vitro and in vivo applications.

Bhowmick Manishabrata M Fields Gregg B GB

Methods in molecular biology (Clifton, N.J.) 20130101

The triple-helical structure of collagen has been accurately reproduced in numerous chemical and recombinant model systems. Triple-helical peptides and proteins have found application for dissecting collagen-stabilizing forces, isolating receptor- and protein-binding sites in collagen, mechanistic examination of collagenolytic proteases, and development of novel biomaterials. Introduction of native-like sequences into triple-helical constructs can reduce the thermal stability of the triple-helix ...[more]

PMID: 24014440

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