Synthesis of heterotrimeric collagen models containing Arg residues in Y-positions and analysis of their conformational stability

Takaki Koide, Yoshimi Nishikawa, Yoshifumi Takahara

研究成果: Article査読

28 被引用数 (Scopus)

抄録

An Arg residue incorporated into the Y-position of collagenous host-guest peptide Ac-(Gly-Pro-Hyp)3-Gly-Pro-Y-(Gly-Pro-Hyp)4-Gly- Gly-NH2 is reported to stabilize the triple helical structure as well as a 4(R)-hydroxyproline (Hyp) residue. Here, we synthesized heterotrimeric collagen models containing Arg in Y-positions utilizing the cystine knot strategy. Analysis of their thermal transition temperatures using circular dichroism spectrometry demonstrated unexpected decrease in the triple helical stability as the number of Arg increased. The obtained results indicated that an Arg residue in a Y-position is not always an equivalent of a Hyp residue, and that it possesses a potential helix destabilizing effect.

本文言語English
ページ(範囲)125-128
ページ数4
ジャーナルBioorganic and Medicinal Chemistry Letters
14
1
DOI
出版ステータスPublished - 2004 1 5
外部発表はい

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Pharmaceutical Science
  • Drug Discovery
  • Clinical Biochemistry
  • Organic Chemistry

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