Metal-assisted stabilization and probing of collagenous triple helices

Takaki Koide; Maki Yuguchi; Mayuka Kawakita; Hiroyuki Konno

doi:10.1021/ja026182+

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 journal › Article › peer-review

46 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 Fe^II(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 language	English
Pages (from-to)	9388-9389
Number of pages	2
Journal	Journal of the American Chemical Society
Volume	124
Issue number	32
DOIs	https://doi.org/10.1021/ja026182+
Publication status	Published - 2002 Aug 14
Externally published	Yes

ASJC Scopus subject areas

Catalysis
Chemistry(all)
Biochemistry
Colloid and Surface Chemistry

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10.1021/ja026182+

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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.",

author = "Takaki Koide and Maki Yuguchi and Mayuka Kawakita and Hiroyuki Konno",

year = "2002",

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doi = "10.1021/ja026182+",

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AU - Yuguchi, Maki

AU - Kawakita, Mayuka

AU - Konno, Hiroyuki

PY - 2002/8/14

Y1 - 2002/8/14

N2 - 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.

AB - 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.

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JF - Journal of the American Chemical Society

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Metal-assisted stabilization and probing of collagenous triple helices

Abstract

ASJC Scopus subject areas

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