Kinetics of glycoxidation of bovine serum albumin by glucose, fructose and ribose and its prevention by food components.

Izabela Sadowska-Bartosz,Sabina Galiniak,Grzegorz Bartosz

doi:10.3390/molecules191118828

Izabela Sadowska-Bartosz, Sabina Galiniak + Show 1 more

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https://doi.org/10.3390/molecules191118828

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Abstract

The aim of this study was to compare the kinetics of the glycoxidation of bovine serum albumin (BSA) as a model protein by three sugars: glucose, fructose and ribose, using fluorometric measurements of the content of advanced glycation end products (AGEs), protein-bound fructosamine, dityrosine, N'-formylkynurenine, kynurenine, tryptophan, the content of advanced oxidation protein products (AOPP), protein carbonyl groups, as well as thiol groups. Moreover, the levels of glycoalbumin and AGEs were determined by using an enzyme-linked immunosorbent assay. Based on the kinetic results, the optimal incubation time for studies of the modification of the glycoxidation rate by additives was chosen, and the effects of 25 compounds of natural origin on the glycoxidation of BSA induced by various sugars were examined. The same compounds were found to have different effects on glycoxidation induced by various sugars, which suggests caution in extrapolation from experiments based on one sugar to other sugars. From among the compounds tested, the most effective inhibitors of glycoxidation were: polyphenols, pyridoxine and 1-cyano-4-hydroxycinnamic acid.

Highlights

In the body, proteins are subject to a variety of enzymatic and non-enzymatic modifications
The behavior of fructosamine followed the same pattern, the higher ribose concentration interfered with the assay (Figure 1C), due to the reaction with nitroblue tetrazolium
We found that standard indices of protein oxidation change in parallel to indices of bovine serum albumin (BSA) glycation

Summary

Introduction

Proteins are subject to a variety of enzymatic and non-enzymatic modifications. One of the unavoidable consequences of metabolism is the non-enzymatic reaction of proteins with reducing sugars (glycation or Maillard reaction). Protein glycation is initiated by a nucleophilic addition reaction between the free amino group from a protein, lipid or nucleic acid and the carbonyl group of reducing saccharides. This reaction forms a reversible Schiff base, which rearranges over a period of days to produce ketoamine or Amadori products. The Amadori products undergo dehydration and rearrangements followed by other reactions, such as cyclization, oxidation and dehydration, to form more stable advanced glycation end products (AGEs) [1]. The accumulation of glycation products is observed in human and animal tissues during aging and is associated with various diseases, including, first of all, diabetes and diabetic nephropathy, microangiopathy and atherosclerosis [4,5]

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