title: 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.
authors.affiliation: Torrey Pines Institute for Molecular Studies, Port St. Lucie, FL, USA.
authors.forename: Manishabrata
authors.initials: M
authors.lastname: Bhowmick
authors.forename: Gregg B
authors.initials: GB
authors.lastname: Fields
mesh_terms: D000596:Amino Acids; D003094:Collagen / Q000737:chemistry*; D005449:Fluorenes; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry*; D011485:Protein Binding; D055550:Protein Stability; D017433:Protein Structure, Secondary
chemical_list: D000596:Amino Acids; D005449:Fluorenes; C016456:N(alpha)-fluorenylmethyloxycarbonylamino acids; D010455:Peptides; D003094:Collagen