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Effects of Resveratrol on the Structure and Catalytic Function of Bovine Liver catalase (BLC): Spectroscopic and Theoretical Studies

Purpose: The study on the interaction between various compounds and macromolecules such as enzymes has been very important for monitoring the alteration of structural and functional properties of them. Resveratrol (3, 5, 4-trihydroxy-stilbene; RES) is a biologically active phytoallexin found in grap...

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Autores principales: Rashtbari, Samaneh, Dehghan, Gholamreza, Yekta, Reza, Jouyban, Abolghasem, Iranshahi, Mehrdad
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Tabriz University of Medical Sciences 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5651055/
https://www.ncbi.nlm.nih.gov/pubmed/29071216
http://dx.doi.org/10.15171/apb.2017.042
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author Rashtbari, Samaneh
Dehghan, Gholamreza
Yekta, Reza
Jouyban, Abolghasem
Iranshahi, Mehrdad
author_facet Rashtbari, Samaneh
Dehghan, Gholamreza
Yekta, Reza
Jouyban, Abolghasem
Iranshahi, Mehrdad
author_sort Rashtbari, Samaneh
collection PubMed
description Purpose: The study on the interaction between various compounds and macromolecules such as enzymes has been very important for monitoring the alteration of structural and functional properties of them. Resveratrol (3, 5, 4-trihydroxy-stilbene; RES) is a biologically active phytoallexin found in grapes and other food products. This article shows an interaction of native bovine liver catalase (BLC) with natural antioxidant product, trans resveratrol (tRES) using multispectroscopic methods. Methods: The interaction between BLC and tRES is performed using UV-vis absorption, fluorescence and circular dichroism (CD) spectroscopy and molecular docking study. Results: In vitro kinetic studies indicated that tRES can decrease BLC activity through uncompetitive inhibition. The results of spectroscopic methods represented that the binding of tRES with BLC can change the micro-region around aromatic amino acids (tryptophan (Trp) and tyrosine (Tyr)) and quench intrinsic fluorescence of BLC by a static mechanism. According to fluorescence quenching data analysis, it was revealed that tRES has one binding site on BLC. The thermodynamic parameters were obtained, which demonstrated that tRES can bind to BLC by van der Waals forces and hydrogen bonds. Molecular docking results indicated that tRES binds to BLC away from heme group and near to the Tyr 324 and Phe 265. These results are in agreement with the experimental results. Conclusion: The inhibitory effect of tRES on BLC demonstrated that excessive consumption of the antioxidants could be resulted in hazardous effects.
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spelling pubmed-56510552017-10-25 Effects of Resveratrol on the Structure and Catalytic Function of Bovine Liver catalase (BLC): Spectroscopic and Theoretical Studies Rashtbari, Samaneh Dehghan, Gholamreza Yekta, Reza Jouyban, Abolghasem Iranshahi, Mehrdad Adv Pharm Bull Research Article Purpose: The study on the interaction between various compounds and macromolecules such as enzymes has been very important for monitoring the alteration of structural and functional properties of them. Resveratrol (3, 5, 4-trihydroxy-stilbene; RES) is a biologically active phytoallexin found in grapes and other food products. This article shows an interaction of native bovine liver catalase (BLC) with natural antioxidant product, trans resveratrol (tRES) using multispectroscopic methods. Methods: The interaction between BLC and tRES is performed using UV-vis absorption, fluorescence and circular dichroism (CD) spectroscopy and molecular docking study. Results: In vitro kinetic studies indicated that tRES can decrease BLC activity through uncompetitive inhibition. The results of spectroscopic methods represented that the binding of tRES with BLC can change the micro-region around aromatic amino acids (tryptophan (Trp) and tyrosine (Tyr)) and quench intrinsic fluorescence of BLC by a static mechanism. According to fluorescence quenching data analysis, it was revealed that tRES has one binding site on BLC. The thermodynamic parameters were obtained, which demonstrated that tRES can bind to BLC by van der Waals forces and hydrogen bonds. Molecular docking results indicated that tRES binds to BLC away from heme group and near to the Tyr 324 and Phe 265. These results are in agreement with the experimental results. Conclusion: The inhibitory effect of tRES on BLC demonstrated that excessive consumption of the antioxidants could be resulted in hazardous effects. Tabriz University of Medical Sciences 2017-09 2017-09-25 /pmc/articles/PMC5651055/ /pubmed/29071216 http://dx.doi.org/10.15171/apb.2017.042 Text en ©2017 The Authors. http://creativecommons.org/licenses/by/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution (CC BY), which permits unrestricted use, distribution, and reproduction in any medium, as long as the original authors and source are cited. No permission is required from the authors or the publishers.
spellingShingle Research Article
Rashtbari, Samaneh
Dehghan, Gholamreza
Yekta, Reza
Jouyban, Abolghasem
Iranshahi, Mehrdad
Effects of Resveratrol on the Structure and Catalytic Function of Bovine Liver catalase (BLC): Spectroscopic and Theoretical Studies
title Effects of Resveratrol on the Structure and Catalytic Function of Bovine Liver catalase (BLC): Spectroscopic and Theoretical Studies
title_full Effects of Resveratrol on the Structure and Catalytic Function of Bovine Liver catalase (BLC): Spectroscopic and Theoretical Studies
title_fullStr Effects of Resveratrol on the Structure and Catalytic Function of Bovine Liver catalase (BLC): Spectroscopic and Theoretical Studies
title_full_unstemmed Effects of Resveratrol on the Structure and Catalytic Function of Bovine Liver catalase (BLC): Spectroscopic and Theoretical Studies
title_short Effects of Resveratrol on the Structure and Catalytic Function of Bovine Liver catalase (BLC): Spectroscopic and Theoretical Studies
title_sort effects of resveratrol on the structure and catalytic function of bovine liver catalase (blc): spectroscopic and theoretical studies
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5651055/
https://www.ncbi.nlm.nih.gov/pubmed/29071216
http://dx.doi.org/10.15171/apb.2017.042
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