TY - JOUR
T1 - Lysine proximity significantly affects glycation of lysine-containing collagen model peptides
AU - Kitamura, Asuka
AU - Matsui, Kouta
AU - Konoki, Keiichi
AU - Matsumori, Nobuaki
AU - Murata, Michio
AU - Kawakami, Toru
AU - Aimoto, Saburo
N1 - Funding Information:
We are grateful to Professor Tohru Oishi, Kyushu University for discussion; to Dr. Sakamoto, Thermo Scientific Co. LTD for recording LC–MS/MS; to Dr. Katsumasa Iijima, Nippi Research Institute of Biomatrix for information on collagen glycation; and to Mr. Hiroaki Yamada for help in experiments. This work was supported in part by Grant-In-Aids for Scientific Research (S) (No. 18101010), and for Scientific Research on Priority Area (A) (No. 12045243) from MEXT, Japan. A research fellowship to A.K. from GCOE program, “Global Education and Research Center for Bio-Environmental Chemistry,” is also acknowledged.
PY - 2011/4/1
Y1 - 2011/4/1
N2 - 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.
AB - 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.
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U2 - 10.1016/j.bmc.2011.02.048
DO - 10.1016/j.bmc.2011.02.048
M3 - Article
C2 - 21429751
AN - SCOPUS:79953203503
SN - 0968-0896
VL - 19
SP - 2125
EP - 2129
JO - Bioorganic and Medicinal Chemistry
JF - Bioorganic and Medicinal Chemistry
IS - 7
ER -
