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

研究成果: Article査読

3 被引用数 (Scopus)


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.

ジャーナルBioorganic and Medicinal Chemistry
出版ステータスPublished - 2011 4 1

ASJC Scopus subject areas

  • 生化学
  • 分子医療
  • 分子生物学
  • 薬科学
  • 創薬
  • 臨床生化学
  • 有機化学


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