Interactions of epicatechin and cysteine with certain other dicarbonyl scavengers during their reaction with methylglyoxal under simulated physiological conditions


DOĞAN CÖMERT E., GÖKMEN V.

FOOD CHEMISTRY, vol.369, 2022 (Peer-Reviewed Journal) identifier identifier identifier

  • Publication Type: Article / Article
  • Volume: 369
  • Publication Date: 2022
  • Doi Number: 10.1016/j.foodchem.2021.130884
  • Journal Name: FOOD CHEMISTRY
  • Journal Indexes: Science Citation Index Expanded, Scopus, Academic Search Premier, PASCAL, Aerospace Database, Aquatic Science & Fisheries Abstracts (ASFA), BIOSIS, CAB Abstracts, Chimica, Communication Abstracts, Compendex, EMBASE, Food Science & Technology Abstracts, MEDLINE, Metadex, Veterinary Science Database, Civil Engineering Abstracts
  • Keywords: Dicarbonyl scavengers, Cysteine, Epicatechin, Methylglyoxal inhibition, Physiological conditions, Synergism, Antagonism, END-PRODUCT FORMATION, TRAPPING METHYLGLYOXAL, GLYCATION, AGENTS, POLYPHENOLS, GLYOXALASE, METABOLISM

Abstract

This study aimed at investigating the effects of interactions between dietary dicarbonyl scavengers coexisting in human plasma on the overall methylglyoxal scavenging potential. Apart from being the most effective dicarbonyl scavengers, epicatechin or cysteine, which can be easily oxidized by other compounds, was reacted with methylglyoxal in the presence of certain other dicarbonyl scavengers under simulated physiological conditions (pH 7.4, 37 degrees C). Methylglyoxal was monitored kinetically in the presence of the individual scavengers or in their combinations with epicatechin or cysteine. The observed and estimated reaction rate constants were calculated for each combination. As the observed rate constant for the reaction between cysteine and epicatechin was found to be significantly greater (p < 0.05) than the estimated rate constant, the results suggest synergism occurred in this combination. Epicatechin was found to interact antagonistically with scavengers that stimulate its oxidation such as creatine, quercetin, and gallic acid during methylglyoxal scavenging.