Collagen model peptides that contain 2,2′-bipyridyl (bpy) ligands were designed and synthesized. The thermal stability of the collagenous triple helix was increased by forming an FeII(bpy-peptide)3 complex. The chirality of the metal center was shifted to form right-handed Δ-isomers induced by the supercoiling of the peptide moiety. Moreover, the refolding rate of the triple helix was increased in the presence of Fe(II). This metal-coordinating system possesses potential to be used to stabilize the triple-helical conformation as well as to probe the folding status of collagen model peptides.
ASJC Scopus subject areas
- Colloid and Surface Chemistry