Metal-assisted stabilization and probing of collagenous triple helices

Takaki Koide, Maki Yuguchi, Mayuka Kawakita, Hiroyuki Konno

Research output: Contribution to journalArticle

60 Citations (Scopus)

Abstract

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
Volume124
Issue number32
DOIs
Publication statusPublished - 2002 Aug 14
Externally publishedYes

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Peptides
Stabilization
Metals
2,2'-Dipyridyl
Collagen
Chirality
Isomers
Conformations
Thermodynamic stability
Hot Temperature
Ligands

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

Metal-assisted stabilization and probing of collagenous triple helices. / Koide, Takaki; Yuguchi, Maki; Kawakita, Mayuka; Konno, Hiroyuki.

In: Journal of the American Chemical Society, Vol. 124, No. 32, 14.08.2002, p. 9388-9389.

Research output: Contribution to journalArticle

Koide, Takaki ; Yuguchi, Maki ; Kawakita, Mayuka ; Konno, Hiroyuki. / Metal-assisted stabilization and probing of collagenous triple helices. In: Journal of the American Chemical Society. 2002 ; Vol. 124, No. 32. pp. 9388-9389.
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