Copper(II)-complexation by non enzymatically glycated peptides
The purpose of our work was to examine the metal binding abilities of selected peptide bound Maillard reaction products (MRPs). The Nα-hippuryl-protected MRPs Nε-fructoselysine and Nε-carboxymethyllysine were synthesised and measurement of stability constants for complexes formed with the physiologi...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Czech Academy of Agricultural Sciences
2004-12-01
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| Series: | Czech Journal of Food Sciences |
| Subjects: | |
| Online Access: | https://cjfs.agriculturejournals.cz/artkey/cjf-200410-0004_copper-ii-complexation-by-non-enzymatically-glycated-peptides.php |
| Summary: | The purpose of our work was to examine the metal binding abilities of selected peptide bound Maillard reaction products (MRPs). The Nα-hippuryl-protected MRPs Nε-fructoselysine and Nε-carboxymethyllysine were synthesised and measurement of stability constants for complexes formed with the physiologically important metal ions copper(II) and zinc(II) was carried out in aqueous solution (T = 298.1 K; I = 0.1M KNO3) using pH-potentiometry. The stability constants of Nε-fructoselysine and Nε-carboxymethyllysine with Cu(II) proved that new coordination centres are formed by the nonenzymatic glycation of proteins. With zinc(II) no complexation was observed. Physiological consequences are discussed, but further studies are necessary in order to clarify the effects of this phenomenon. |
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| ISSN: | 1212-1800 1805-9317 |