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Experimental and hypothetical appraisal on inhibition of glucose-induced glycation of bovine serum albumin by quercetin

BACKGROUND: The specificity of protein functions depends on its folding ability into a functional structure. Protein folding is an essential systemic phenomenon that prevents incorrect folding which could result in harmful aggregation. This harmful aggregation of proteins causes neurodegenerative di...

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Autores principales: Oso, Babatunde Joseph, Olaoye, Ige, Oso, Olufunke Temiloluwa
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Berlin Heidelberg 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10654330/
https://www.ncbi.nlm.nih.gov/pubmed/37971629
http://dx.doi.org/10.1186/s43141-023-00588-5
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author Oso, Babatunde Joseph
Olaoye, Ige
Oso, Olufunke Temiloluwa
author_facet Oso, Babatunde Joseph
Olaoye, Ige
Oso, Olufunke Temiloluwa
author_sort Oso, Babatunde Joseph
collection PubMed
description BACKGROUND: The specificity of protein functions depends on its folding ability into a functional structure. Protein folding is an essential systemic phenomenon that prevents incorrect folding which could result in harmful aggregation. This harmful aggregation of proteins causes neurodegenerative diseases and systemic amyloidosis. Experimental and theoretical approaches were used in this study to explicate the probable mechanisms of action of quercetin in inhibition of glucose-induced glycation through estimations of percentage glycated protein, inhibited induced protein aggregation, and unoxidized bovine serum albumin thiol groups and assessments of molecular interactions of quercetin with the structures of bovine serum albumin, amyloid beta-peptide (1–42) and 3D amyloid-beta (1–42) fibrils retrieved from the protein databank (http://www.rcsb.org). RESULTS: The results showed quercetin inhibited the formation of glycated protein, protein aggregation, and thiol oxidation in a concentration-dependent manner where 200 μg/ml showed the highest inhibition while 50 μg/ml depicted the least inhibition in all the studied assessments. From the docking analysis, it was observed that quercetin had a significantly higher binding affinities − 8.67 ± 0.09 kcal/mol, − 5.37 ± 0.05 kcal/mol and − 5.93 ± 0.13 kcal/mol for the bovine serum albumin, amyloid beta-peptide (1–42) and 3D amyloid-beta (1–42) fibrils respectively compared to the glucose, the inducer. Quercetin and glucose interacted with amino acid residues at the BSA subdomain IIA thus providing a clue that quercetin may impose its inhibition through the binding domain. Also, it is important to mention that the phytochemicals shared a similar interaction profile as that of glucose with the amyloid-beta. CONCLUSIONS: These findings established the beneficial effects of quercetin as a potential agent that could alleviate hyperglycaemic-initiated disorders associated with elevated serum glucose levels.
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spelling pubmed-106543302023-11-16 Experimental and hypothetical appraisal on inhibition of glucose-induced glycation of bovine serum albumin by quercetin Oso, Babatunde Joseph Olaoye, Ige Oso, Olufunke Temiloluwa J Genet Eng Biotechnol Research BACKGROUND: The specificity of protein functions depends on its folding ability into a functional structure. Protein folding is an essential systemic phenomenon that prevents incorrect folding which could result in harmful aggregation. This harmful aggregation of proteins causes neurodegenerative diseases and systemic amyloidosis. Experimental and theoretical approaches were used in this study to explicate the probable mechanisms of action of quercetin in inhibition of glucose-induced glycation through estimations of percentage glycated protein, inhibited induced protein aggregation, and unoxidized bovine serum albumin thiol groups and assessments of molecular interactions of quercetin with the structures of bovine serum albumin, amyloid beta-peptide (1–42) and 3D amyloid-beta (1–42) fibrils retrieved from the protein databank (http://www.rcsb.org). RESULTS: The results showed quercetin inhibited the formation of glycated protein, protein aggregation, and thiol oxidation in a concentration-dependent manner where 200 μg/ml showed the highest inhibition while 50 μg/ml depicted the least inhibition in all the studied assessments. From the docking analysis, it was observed that quercetin had a significantly higher binding affinities − 8.67 ± 0.09 kcal/mol, − 5.37 ± 0.05 kcal/mol and − 5.93 ± 0.13 kcal/mol for the bovine serum albumin, amyloid beta-peptide (1–42) and 3D amyloid-beta (1–42) fibrils respectively compared to the glucose, the inducer. Quercetin and glucose interacted with amino acid residues at the BSA subdomain IIA thus providing a clue that quercetin may impose its inhibition through the binding domain. Also, it is important to mention that the phytochemicals shared a similar interaction profile as that of glucose with the amyloid-beta. CONCLUSIONS: These findings established the beneficial effects of quercetin as a potential agent that could alleviate hyperglycaemic-initiated disorders associated with elevated serum glucose levels. Springer Berlin Heidelberg 2023-11-16 /pmc/articles/PMC10654330/ /pubmed/37971629 http://dx.doi.org/10.1186/s43141-023-00588-5 Text en © The Author(s) 2023 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Research
Oso, Babatunde Joseph
Olaoye, Ige
Oso, Olufunke Temiloluwa
Experimental and hypothetical appraisal on inhibition of glucose-induced glycation of bovine serum albumin by quercetin
title Experimental and hypothetical appraisal on inhibition of glucose-induced glycation of bovine serum albumin by quercetin
title_full Experimental and hypothetical appraisal on inhibition of glucose-induced glycation of bovine serum albumin by quercetin
title_fullStr Experimental and hypothetical appraisal on inhibition of glucose-induced glycation of bovine serum albumin by quercetin
title_full_unstemmed Experimental and hypothetical appraisal on inhibition of glucose-induced glycation of bovine serum albumin by quercetin
title_short Experimental and hypothetical appraisal on inhibition of glucose-induced glycation of bovine serum albumin by quercetin
title_sort experimental and hypothetical appraisal on inhibition of glucose-induced glycation of bovine serum albumin by quercetin
topic Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10654330/
https://www.ncbi.nlm.nih.gov/pubmed/37971629
http://dx.doi.org/10.1186/s43141-023-00588-5
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