Stabilization of Collagen-Model, Triple-Helical Peptides for In Vitro and In Vivo Applications
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Last Update: 2020-12-24
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Source: Internet
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Author: User
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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-helixto below that of the physiological environment. In turn, incorporation of nonnative amino acids and/or templates can enhancetriple-helix stability. We presently describe approaches by which triple-helical structure can be modulated for use underphysiological or near-physiological conditions.
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