Lysine proximity significantly affects glycation of lysine-containing collagen model peptides

Asuka Kitamura, Kouta Matsui, Keiichi Konoki, Nobuaki Matsumori, Michio Murata, Toru Kawakami, Saburo Aimoto

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

Advanced glycation end products (AGE) are known to cause diabetes complications in hyperglycemia patients. In this study we prepared hetero-trimers of collagen model peptides comprising Ac-(Pro-Hyp-Gly) 5-Pro-Lys-Gly-(Pro-Hyp-Gly)5-Ala-NH2 (4) and Ac-(Pro-Hyp-Gly)11-Ala-NH2 (5) to investigate the clustering effect of lysine on AGE formation. The formation rate of carboxymethyllysine over several months was determined for the mixtures of peptides 4 and 5 at (3:0), (2:1) and (1:2) in the presence of glucose. The contents of carboxymethyllysine were significantly enhanced for (3:0) and (2:1) as compared with (1:2), suggesting that the proximity of lysine residues in the trimers accelerated formation of the AGE. Furthermore, a lysine dimerization moiety (GOLD) was identified for the first time from AGEs of glucose origin, which implied the significance of GOLD in oligomerization of collagens and other long-life proteins.

Original languageEnglish
Pages (from-to)2125-2129
Number of pages5
JournalBioorganic and Medicinal Chemistry
Volume19
Issue number7
DOIs
Publication statusPublished - 2011 Apr 1

Keywords

  • Carboxymethyllysine
  • Collagen
  • Glycation end products
  • Glyoxal lysine dimer

ASJC Scopus subject areas

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

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