Fructose and methylglyoxal-induced glycation alters structural and functional properties of salivary proteins, albumin and lysozyme.
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 s...
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2022-01-01
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| Series: | PLoS ONE |
| Online Access: | https://doi.org/10.1371/journal.pone.0262369 |
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| author | Mariane Yumiko Muraoka Allisson Benatti Justino Douglas Carvalho Caixeta Julia Silveira Queiroz Robinson Sabino-Silva Foued Salmen Espindola |
| author_facet | Mariane Yumiko Muraoka Allisson Benatti Justino Douglas Carvalho Caixeta Julia Silveira Queiroz Robinson Sabino-Silva Foued Salmen Espindola |
| author_sort | Mariane Yumiko Muraoka |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-12-20T16:56:48Z |
| format | Article |
| id | doaj.art-ff84a21887ed452e9605b51cfd6248d7 |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-20T16:56:48Z |
| publishDate | 2022-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-ff84a21887ed452e9605b51cfd6248d72022-12-21T19:32:42ZengPublic Library of Science (PLoS)PLoS ONE1932-62032022-01-01171e026236910.1371/journal.pone.0262369Fructose and methylglyoxal-induced glycation alters structural and functional properties of salivary proteins, albumin and lysozyme.Mariane Yumiko MuraokaAllisson Benatti JustinoDouglas Carvalho CaixetaJulia Silveira QueirozRobinson Sabino-SilvaFoued Salmen EspindolaGlycation 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.https://doi.org/10.1371/journal.pone.0262369 |
| spellingShingle | Mariane Yumiko Muraoka Allisson Benatti Justino Douglas Carvalho Caixeta Julia Silveira Queiroz Robinson Sabino-Silva Foued Salmen Espindola Fructose and methylglyoxal-induced glycation alters structural and functional properties of salivary proteins, albumin and lysozyme. PLoS ONE |
| title | Fructose and methylglyoxal-induced glycation alters structural and functional properties of salivary proteins, albumin and lysozyme. |
| title_full | Fructose and methylglyoxal-induced glycation alters structural and functional properties of salivary proteins, albumin and lysozyme. |
| title_fullStr | Fructose and methylglyoxal-induced glycation alters structural and functional properties of salivary proteins, albumin and lysozyme. |
| title_full_unstemmed | Fructose and methylglyoxal-induced glycation alters structural and functional properties of salivary proteins, albumin and lysozyme. |
| title_short | Fructose and methylglyoxal-induced glycation alters structural and functional properties of salivary proteins, albumin and lysozyme. |
| title_sort | fructose and methylglyoxal induced glycation alters structural and functional properties of salivary proteins albumin and lysozyme |
| url | https://doi.org/10.1371/journal.pone.0262369 |
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