Naslov
Fructose induced N-terminal glycation of enkephalins and related peptides

Autori
Jakas, Andreja ; Vinković, Marijana ; Smrečki, Vilko ; Šporec, Maja ; Horvat, Štefica

Izvornik
Journal of Peptide Science (1075-2617) 14 (2008), 8; 936-945

Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni

Ključne riječi
enkephalin; fructose; glycation; Heyns compound; imidazolidinone; Maillard reaction; peptide stability; reducing sugar

Sažetak
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 was 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 result of different configuration at the newly formed stereogenic center, large stability differences in the 2S* and 2R* isomers of the imidazolidinone compounds were observed.

Izvorni jezik
Engleski

Znanstvena područja
Kemija

POVEZANOST RADA