Abstract
Glycation process refers to reactions between reduction sugars and amino acids that can lead to formation of advanced glycation end products (AGEs) which are related to changes in chemical and functional properties of biological structures that accumulate during aging and diseases. The aim of this study was to perform and analyze in vitro glycation by fructose and methylglyoxal (MGO) using salivary fluid, albumin, lysozyme, and salivary α-amylase (sAA). Glycation effect was analyzed by biochemical and spectroscopic methods. The results were obtained by fluorescence analysis, infrared spectroscopy (total attenuated reflection—Fourier transform, ATR-FTIR) followed by multivariate analysis of principal components (PCA), protein profile, immunodetection, enzymatic activity and oxidative damage to proteins. Fluorescence increased in all glycated samples, except in saliva with fructose. The ATR-FTIR spectra and PCA analysis showed structural changes related to the vibrational mode of glycation of albumin, lysozyme, and salivary proteins. Glycation increased the relative molecular mass (Mr) in protein profile of albumin and lysozyme. Saliva showed a decrease in band intensity when glycated. The analysis of sAA immunoblotting indicated a relative reduction in intensity of its correspondent Mr after sAA glycation; and a decrease in its enzymatic activity was observed. Carbonylation levels increased in all glycated samples, except for saliva with fructose. Thiol content decreased only for glycated lysozyme and saliva with MGO. Therefore, glycation of salivary fluid and sAA may have the potential to identify products derived by glycation process. This opens perspectives for further studies on the use of saliva, an easy and non-invasive collection fluid, to monitor glycated proteins in the aging process and evolution of diseases.
Highlights
In order to evaluate spectral differences related to glycation process with fructose and MGO after incubation of 21 days, spectra of samples were submitted to Principal component analysis (PCA) analysis
Results of salivary α-amylase (sAA) showed a significant increase in fluorescence intensity due to glycation promoted by incubation with fructose and MGO
As a method used to analyze structural changes in molecules, attenuated total reflectance component (ATR)-FTIR spectroscopy clearly indicated changes in the structure of albumin, lysozyme and saliva caused by glycation by both fructose and MGO
Summary
Glycation process refers to a sequence of non-enzymatic reactions that begin when reducing sugars such as glucose and fructose react with nucleophilic groups of amino acids from. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript
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