Metal-assisted stabilization and probing of collagenous triple helices.
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 Fe(II)(bpy-peptide)(3) complex. The chirality of the metal center was shifted to form right-handed Delta-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.
Koide
Takaki
T
Department of Biological Science and Technology, Faculty of Engineering, The University of Tokushima, Japan. tkoide@bio.tokushima-u.ac.jp
Yuguchi
Maki
M
Kawakita
Mayuka
M
Konno
Hiroyuki
H
D003094:Collagen / Q000737:chemistry*; D008670:Metals / Q000737:chemistry*; D015335:Molecular Probes
D008670:Metals; D015335:Molecular Probes; D003094:Collagen