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Fructose‐induced N ‐terminal glycation of enkephalins and related peptides
Author(s) -
Jakas Andreja,
Vinković Marijana,
Smrečki Vilko,
Šporec Maja,
Horvat Štefica
Publication year - 2008
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.1029
Subject(s) - glycation , chemistry , biochemistry , fructose , terminal (telecommunication) , pharmacology , receptor , medicine , telecommunications , computer science
The formation of glycation products in model systems consisting of fructose and the endogenous opioid peptides not containing lysine residue, such as Leu‐enkephalin (Tyr‐Gly‐Gly‐Phe‐Leu) and Met‐enkephalin (Tyr‐Gly‐Gly‐Phe‐Met), or of their fragments, Tyr‐Gly‐Gly‐Phe and Tyr‐Gly‐Gly, was examined. N ‐(2‐Deoxy‐aldos‐2‐yl)‐peptides (Heyns compounds) as well as diastereoisomeric imidazolidinone compounds were identified as reaction products of N ‐terminal amino group glycation for each of the peptides studied. The structure of the glycation products and relative configuration of C‐2 substituents on the imidazolidinone ring in diastereoisomers were determined by NMR experiments. The chemical and enzymatic stability of the fructose‐derived glycated products of Leu‐ and Met‐enkephalin was studied in phosphate‐buffered saline (pH 7.4) and in human serum at 37 °C. The obtained results revealed that glycation increases the stability of the parent peptide to enzymatic degradation. As a result of different configuration at the newly formed stereogenic center, large stability differences in the 2 S * and 2 R * isomers of the imidazolidinone compounds were observed. Copyright © 2008 European Peptide Society and John Wiley & Sons, Ltd.