201. Lysine proximity significantly affects glycation of lysine-containing collagen model peptides
- Author
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Asuka Kitamura, Nobuaki Matsumori, Saburo Aimoto, Toru Kawakami, Kouta Matsui, Michio Murata, and Keiichi Konoki
- Subjects
Glycation End Products, Advanced ,Glycosylation ,Clinical Biochemistry ,Lysine ,Pharmaceutical Science ,Biochemistry ,Mass Spectrometry ,chemistry.chemical_compound ,Structure-Activity Relationship ,Glycation ,Diabetes mellitus ,Drug Discovery ,medicine ,Structure–activity relationship ,Moiety ,Humans ,Formation rate ,Molecular Biology ,Chemistry ,Organic Chemistry ,Lysine metabolism ,medicine.disease ,Peptide Fragments ,Molecular Medicine ,Collagen ,Peptides - 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-NH(2) (4) and Ac-(Pro-Hyp-Gly)(11)-Ala-NH(2) (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.
- Published
- 2011