Abstract
Advanced Glycation End-Products (AGEs) are created in the last step of protein glycation and can be a factor in aging and in the development or worsening of many degenerative diseases (diabetes, chronic kidney disease, atherosclerosis, Alzheimer’s disease, etc.). Albumin is the most susceptible to glycation plasma protein. Modified albumin by AGEs may be more resistant to enzymatic degradation, which further increases the local accumulation of AGEs in tissues. The aim of the present study was to analyze in vitro glycation of serum albumin in the presence of piracetam (PIR) and the gliclazide (GLZ)-glycated albumin interaction. The analysis of PIR as an inhibitor and GLZ interaction with nonglycated human albumin (HSA) and glycated by fructose human albumin (gHSAFRC), in the absence and presence of piracetam (gHSAFRC-PIR), was performed by fluorescence quenching of macromolecules. On the basis of obtained data we concluded that under the influence of glycation, association constant () of gliclazide to human serum albumin decreases and GLZ binds to HSA with less strength than under physiological conditions. PIR strongly inhibited the formation of AGEs in the system where the efficiency of HSA glycation was the largest. The analysis of piracetam influence on the GLZ-glycated albumin interaction has shown that piracetam increases the binding strength of GLZ to glycated albumin and weakens its therapeutic effect. Based on the obtained data we concluded that monitoring therapy and precautions are required in the treatment when the combinations of gliclazide and piracetam are used at the same time.
Highlights
Diabetes, as the only noninfectious disease, was recognized by the UNO as an epidemic of the XXI century
Based on the obtained data we concluded that monitoring therapy and precautions are required in the treatment when the combinations of gliclazide and piracetam are used at the same time
Different properties that play a significant role in the pathology of diabetes and its associated diseases
Summary
As the only noninfectious disease, was recognized by the UNO as an epidemic of the XXI century. The International Diabetes Federation (IDF) estimates that the number of people with diabetes in 2035 increases to 592 million [1]. Due to the long-term course of the disease, damage, dysfunctions, and insufficiency of many tissues and organs occur. The main factor responsible for the organ complications of diabetes, i.e., macro- and microangiopathy, is an increase in the concentration of reducing sugars in the blood. The carbonyl group of reducing sugar (including glucose, fructose, and galactose), in a series of transformations called Maillard reactions, reacts with the primary free amino group of the NH2 -terminal residue of the protein or the lysine (Lys) and arginine (Arg) residues, causing their glycation [2,3]. The protein glycation process is multistep; in the last stage, Advanced Glycation
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