Selective covalent capture of collagen triple helices with a minimal protecting group strategy.

ABSTRACT: Collagens and their most characteristic structural unit, the triple helix, play many critical roles in living systems which drive interest in preparing mimics of them. However, application of collagen mimetic helices is limited by poor thermal stability, slow rates of folding and poor equilibrium between monomer and trimer. Covalent capture of the self-assembled triple helix can solve these problems while preserving the native three-dimensional structure critical for biological function. Covalent capture takes advantage of strategically placed lysine and glutamate (or aspartate) residues which form stabilizing charge-pair interactions in the supramolecular helix and can subsequently be converted to isopeptide amide bonds under folded, aqueous conditions. While covalent capture is powerful,

SUBMITTER: Yu LT 

PROVIDER: S-EPMC8890135 | biostudies-literature | 2022 Mar

REPOSITORIES: biostudies-literature