Photo-responsive azobenzene interactions promote hierarchical self-assembly of collagen triple-helical peptides to various higher-order structures.

ABSTRACT: Collagen is an essential structural protein in animal tissues and plays key roles in cellular modulation. We investigated methods to discover collagen model peptides (CMPs) that would self-assemble into triple helices and then grow into supramolecular organizations with diverse morphological features, which would be valuable as biomaterials. This challenging undertaking was achieved by placing azobenzene groups on the ends of the CMPs, (GPO) _n (n = 3-10), Azo-(GPO) _n . In a dilute aqueous solution (80 μM), CD spectra indicated that the Azo-(GPO) _n (n > 4) formed triple helices due to strong hydrophobic azobenzene interactions, and that helix stability was increased with the peptide segment length. The resulting triple heli

SUBMITTER: Higashi N 

PROVIDER: S-EPMC9052399 | biostudies-literature | 2020 Apr

REPOSITORIES: biostudies-literature