ArticlePloS one2022
Fructose and methylglyoxal-induced glycation alters structural and functional properties of salivary proteins, albumin and lysozyme.
Article in PloS one, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 28 citations in OpenAlex.
- Label-Free Evaluation of Advanced Glycation End Products by a Comprehensive Biophysical Analysis.Analytical chemistry · 2026Article
- Modulation of Advanced Glycation End Products and Oxidative Stress by Hesperetin-7-Pharmaceuticals (Basel, Switzerland) · 2026Article
- Correlation Between Advanced Glycation End Products and Ultrasonographic Measurements of Cervico-Facial Skin Tissue.Diagnostics (Basel, Switzerland) · 2026Article
- Salivary protein adsorption on titanium abutments: a comparative study of edentulous and partially edentulous patients.Frontiers in oral health · 2026Article
- Revisiting Pt foil catalysts for formamide electrosynthesis achieved at industrial-level current densities.Nature communications · 2025Article
- Saliva as a Diagnostic Tool for Systemic Diseases-A Narrative Review.Medicina (Kaunas, Lithuania) · 2025Review
- Interaction between albumin originating from persons with uncontrolled diabetes mellitus type 2 and food antioxidants.ADMET & DMPK · 2025Article
- Methylglyoxal: A Key Factor for Diabetic Retinopathy and Its Effects on Retinal Damage.Biomedicines · 2024Review
- The Synergistic Effects of Polyol Pathway-Induced Oxidative and Osmotic Stress in the Aetiology of Diabetic Cataracts.International journal of molecular sciences · 2024Review
- Advanced Glycation End-Products Acting as Immunomodulators for Chronic Inflammation, Inflammaging and Carcinogenesis in Patients with Diabetes and Immune-Related Diseases.Biomedicines · 2024Review
- Novel Fluorometric Assay of Antiglycation Activity Based on Methylglyoxal-Induced Protein Carbonylation.Antioxidants (Basel, Switzerland) · 2023Article
- The Post-Translational Modifications of Human Salivary Peptides and Proteins Evidenced by Top-Down Platforms.International journal of molecular sciences · 2023Review
- Probing local changes to α-helical structures with 2D IR spectroscopy and isotope labeling.Biophysical journal · 2023Article
- Salivary Detection of Zika Virus Infection Using ATR-FTIR Spectroscopy Coupled with Machine Learning Algorithms and Univariate Analysis: A Proof-of-Concept Animal Study.Diagnostics (Basel, Switzerland) · 2023Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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.
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