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

Takaki Koide*, Yoshimi Nishikawa, Yoshifumi Takahara

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

29 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)125-128
Number of pages4
JournalBioorganic and Medicinal Chemistry Letters
Volume14
Issue number1
DOIs
Publication statusPublished - 2004 Jan 5
Externally publishedYes

ASJC Scopus subject areas

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

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