Abstract
Advanced glycation end products (AGEs) are involved in the aging and the development of common chronic diseases. Hydroxytyrosol (HT) and its acetate derivative (HTA) exert a significant inhibitory activity on the formation of fluorescent AGEs in bovine serum albumin glycation model systems induced by methylglyoxal (IC50 value of 0.48 and 0.58 ”mol/mL, respectively) and glucose (IC50 2.30 and 2.92 ”mol/mL, respectively). Furthermore, HT and HTA showed a relevant carbonyl scavenging capacity toward methylglyoxal and glyoxal, which are the most potent promoters of the glycation in vivo, at molar reaction rates from 0.2 to 10 (carbonyl:phenol). However, carbonyl trapping capacity was significantly more effective against methylglyoxal (IC50 0.19 ”mol/mL) than glyoxal (IC50 0.26 ”mol/mL). At equimolar concentrations, the ester linkage did not significantly affect the antiglycative activity and carbonyl trapping capacity of the orthodiphenolic ring structure. Results were confirmed with the specific inhibition of the formation of the principal AGEs. Formation of carboxymethyl-lysine, argpyrimidine and carboxyethyl-lysine was significantly reduced by 61.9, 71.4 and 20.9 %, respectively. HT and its esters could be considered for upscaling studies as promising natural strategy against adverse consequences of protein glycation.
Highlights
Glycation occurs physiologically in the course of aging with the formation of advanced glycation end products (AGEs) when a free amino group of protein interacts with the carbonyl group of glucose [1]
The antiglycative activity of HT and hydroxytyrosol acetate (HTA) was evaluated by measuring the inhibition of the formation of fluorescent AGEs in a model of glycation with bovine serum albumin (BSA) under physiological conditions
Glycation reaction in the BSAâGLC system proceeds slower than the BSAâMGO system since autoxidation of glucose to form dicarbonyl compounds is minimized in the presence of EDTA
Summary
Glycation occurs physiologically in the course of aging with the formation of advanced glycation end products (AGEs) when a free amino group of protein interacts with the carbonyl group of glucose [1]. Dicarbonyl compounds, such as methylglyoxal (MGO) and glyoxal (GO), are formed from the sugar degradation being key intermediates in AGEs formation [2]. AGEs that accumulate in tissue altering irreversibly the functionality and protein structure by binding to certain amino acids such as lysine and arginine are structurally modified [2]. AGEs might damage the tissues and organs underlying inflammation through specific receptor, and its accumulation is accelerated in diabetes, neurodegenerative and autoimmune diseases. AGEs have been associated with the process of normal aging and the
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