Supramolecular assembly of electrostatically stabilized, hydroxyproline-lacking collagen-mimetic peptides.

ABSTRACT: The mechanical and biological functions of the native collagens remain an inspiration in materials design, but widespread application of de novo collagens has been limited in part by the need for hydroxylated proline in the formation of stable triple helical structures. To address this continued need and to expand the potential for recombinant expression of functional, hydroxyproline-lacking collagen-mimetic peptides, we have designed a hydrophilic, nonrepetitive, and thermally stable collagen-mimetic peptide via the incorporation of triple-helix-stabilizing charged triplets. The peptide sequence is also equipped with a type III-collagen-mimetic cystine knot at the C-terminus to facilitate covalent cross-linking of the triple helix via simple air oxidation. Circular dichroic spectroscopy (

SUBMITTER: Krishna OD 

PROVIDER: S-EPMC2751732 | biostudies-literature | 2009 Sep

REPOSITORIES: biostudies-literature