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Copper(II)-complexation by non enzymatically glycated peptides

Author

Listed:
  • S. T Seifert

    (Institute of Food Chemistry and)

  • R. Krause

    (Institute of Food Chemistry and)

  • K. Gloe

    (Institute of Food Chemistry and)

  • T. Henle

    (Institute of Food Chemistry and)

Abstract

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.

Suggested Citation

  • S. T Seifert & R. Krause & K. Gloe & T. Henle, 2004. "Copper(II)-complexation by non enzymatically glycated peptides," Czech Journal of Food Sciences, Czech Academy of Agricultural Sciences, vol. 22(SpecialIs), pages 106-108.
    • Handle: RePEc:caa:jnlcjf:v:22:y:2004:i:specialissue:id:10628-cjfs
    DOI: 10.17221/10628-CJFS
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