2011年4月
Lysine proximity significantly affects glycation of lysine-containing collagen model peptides
BIOORGANIC & MEDICINAL CHEMISTRY
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- 巻
- 19
- 号
- 7
- 開始ページ
- 2125
- 終了ページ
- 2129
- 記述言語
- 英語
- 掲載種別
- DOI
- 10.1016/j.bmc.2011.02.048
- 出版者・発行元
- PERGAMON-ELSEVIER SCIENCE LTD
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. (C) 2011 Elsevier Ltd. All rights reserved.
- リンク情報
- ID情報
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- DOI : 10.1016/j.bmc.2011.02.048
- ISSN : 0968-0896
- Web of Science ID : WOS:000288792400002