Metal-assisted stabilization and probing of collagenous triple helices

Takaki Koide*, Maki Yuguchi, Mayuka Kawakita, Hiroyuki Konno

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

46 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)9388-9389
Number of pages2
JournalJournal of the American Chemical Society
Issue number32
Publication statusPublished - 2002 Aug 14
Externally publishedYes

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry


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