TY - JOUR
T1 - Intact glycation end products containing carboxymethyl-lysine and glyoxal lysine dimer obtained from synthetic collagen model peptide
AU - Yamada, Hiroaki
AU - Sasaki, Tomoko
AU - Niwa, Sachiko
AU - Oishi, Tohru
AU - Murata, Michio
AU - Kawakami, Toru
AU - Aimoto, Saburo
N1 - Funding Information:
We are grateful to Dr. Nobuaki Matsumori in authors’ laboratory (M.M.) for discussion; and to Dr. Katsumasa Iijima, Nippi Research Institute of Biomatrix for information on collagen glycation. This work was supported in part by a Grant-In-Aid for Scientific Research on Priority Area (A) (No. 12045243) from MEXT, Japan.
PY - 2004/11/15
Y1 - 2004/11/15
N2 - Glycation reactions using a model peptide of collagen and glucose or ribose resulted in detection of carboxylmethyl-lysine in the peptide; and treatment with glyoxal provided a dimer of the peptide linked with glyoxal lysine dimer (GOLD). Advanced glycation end products (AGE) are accumulated in human tissues when long-lived proteins are glycated due to hyperglycemia and/or aging. In this study, we synthesized a collagen model peptide, Ac-(Pro-Hyp-Gly) 5-Pro-Lys-Gly-(Pro-Hyp-Gly) 5-Ala-NH 2 to investigate intact AGEs in peptides. The peptide formed a stable triple helix structure, and was subjected to glycation reactions with glucose, ribose and glyoxal. Besides carboxymethyl-lysine in the peptide, a conjugated form linked with glyoxal lysine dimer (GOLD) was detected upon treatment with glyoxal. This is the first example of intact glycation-derived dimers of peptides retaining intrinsic protein structures.
AB - Glycation reactions using a model peptide of collagen and glucose or ribose resulted in detection of carboxylmethyl-lysine in the peptide; and treatment with glyoxal provided a dimer of the peptide linked with glyoxal lysine dimer (GOLD). Advanced glycation end products (AGE) are accumulated in human tissues when long-lived proteins are glycated due to hyperglycemia and/or aging. In this study, we synthesized a collagen model peptide, Ac-(Pro-Hyp-Gly) 5-Pro-Lys-Gly-(Pro-Hyp-Gly) 5-Ala-NH 2 to investigate intact AGEs in peptides. The peptide formed a stable triple helix structure, and was subjected to glycation reactions with glucose, ribose and glyoxal. Besides carboxymethyl-lysine in the peptide, a conjugated form linked with glyoxal lysine dimer (GOLD) was detected upon treatment with glyoxal. This is the first example of intact glycation-derived dimers of peptides retaining intrinsic protein structures.
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U2 - 10.1016/j.bmcl.2004.08.044
DO - 10.1016/j.bmcl.2004.08.044
M3 - Article
C2 - 15482946
AN - SCOPUS:5144232197
SN - 0960-894X
VL - 14
SP - 5677
EP - 5680
JO - Bioorganic and Medicinal Chemistry Letters
JF - Bioorganic and Medicinal Chemistry Letters
IS - 22
ER -