LAUSR.org creates dashboard-style pages of related content for over 1.5 million academic articles. Sign Up to like articles & get recommendations!

Copper(II)-complexation by non enzymatically glycated peptides

Photo from academic.microsoft.com

The purpose of our work was to examine the metal binding abilities of selected peptide bound Maillard reaction products (MRPs). The N"-hippuryl-protected MRPs N'-fructoselysine and N e -carboxymethyllysine were synthesisedand… Click to show full abstract

The purpose of our work was to examine the metal binding abilities of selected peptide bound Maillard reaction products (MRPs). The N"-hippuryl-protected MRPs N'-fructoselysine and N e -carboxymethyllysine were synthesisedand 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 KNO 3 ) using pH-potentiometry. The stability constants of N'-fructoselysine and N e -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.

Keywords: non enzymatically; complexation; copper; enzymatically glycated; complexation non; copper complexation

Journal Title: Czech Journal of Food Sciences
Year Published: 2018

Link to full text (if available)


Share on Social Media:                               Sign Up to like & get
recommendations!

Related content

More Information              News              Social Media              Video              Recommended



                Click one of the above tabs to view related content.