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Interactions of cephalexin with bovine serum albumin: displacement reaction and molecular docking

[Image: see text] Introduction: The drug-plasma protein interaction is a fundamental issue in guessing and checking the serious drug side effects related with other drugs. The purpose of this research was to study the interaction of cephalexin with bovine serum albumin (BSA) and displacement reactio...

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Autores principales: Hamishehkar, Hamed, Hosseini, Soheila, Naseri, Abdolhossein, Safarnejad, Azam, Rasoulzadeh, Farzaneh
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Tabriz University of Medical Sciences 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5108985/
https://www.ncbi.nlm.nih.gov/pubmed/27853676
http://dx.doi.org/10.15171/bi.2016.19
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author Hamishehkar, Hamed
Hosseini, Soheila
Naseri, Abdolhossein
Safarnejad, Azam
Rasoulzadeh, Farzaneh
author_facet Hamishehkar, Hamed
Hosseini, Soheila
Naseri, Abdolhossein
Safarnejad, Azam
Rasoulzadeh, Farzaneh
author_sort Hamishehkar, Hamed
collection PubMed
description [Image: see text] Introduction: The drug-plasma protein interaction is a fundamental issue in guessing and checking the serious drug side effects related with other drugs. The purpose of this research was to study the interaction of cephalexin with bovine serum albumin (BSA) and displacement reaction using site probes. Methods: The interaction mechanism concerning cephalexin (CPL) with BSA was investigated using various spectroscopic methods and molecular modeling method. The binding sites number, n, apparent binding constant, K, and thermodynamic parameters, ΔG(0), ΔH(0), and ΔS(0) were considered at different temperatures. To evaluate the experimental results, molecular docking modeling was calculated. Results: The distance, r=1.156 nm between BSA and CPL were found in accordance with the Forster theory of non-radiation energy transfer (FRET) indicating energy transfer occurs between BSA and CPL. According to the binding parameters and ΔG(0)= negative values and ΔS(0)= 28.275 j mol(-1)K(-1), a static quenching process is effective in the CPL-BSA interaction spontaneously. ΔG(0) for the CPL-BSA complex obtained from the docking simulation is -28.99 kj mol(-1), which is close to experimental ΔG of binding, -21.349 kj mol(-1) that indicates a good agreement between the results of docking methods and experimental data. Conclusion: The outcomes of spectroscopic methods revealed that the conformation of BSA changed during drug-BSA interaction. The results of FRET propose that CPL quenches the fluorescence of BSA by static quenching and FRET. The displacement study showed that phenylbutazon and ketoprofen displaced CPL, indicating that its binding site on albumin is site I and Gentamicin cannot be displaced from the binding site of CPL. All results of molecular docking method agreed with the results of experimental data.
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spelling pubmed-51089852016-11-16 Interactions of cephalexin with bovine serum albumin: displacement reaction and molecular docking Hamishehkar, Hamed Hosseini, Soheila Naseri, Abdolhossein Safarnejad, Azam Rasoulzadeh, Farzaneh Bioimpacts Original Article [Image: see text] Introduction: The drug-plasma protein interaction is a fundamental issue in guessing and checking the serious drug side effects related with other drugs. The purpose of this research was to study the interaction of cephalexin with bovine serum albumin (BSA) and displacement reaction using site probes. Methods: The interaction mechanism concerning cephalexin (CPL) with BSA was investigated using various spectroscopic methods and molecular modeling method. The binding sites number, n, apparent binding constant, K, and thermodynamic parameters, ΔG(0), ΔH(0), and ΔS(0) were considered at different temperatures. To evaluate the experimental results, molecular docking modeling was calculated. Results: The distance, r=1.156 nm between BSA and CPL were found in accordance with the Forster theory of non-radiation energy transfer (FRET) indicating energy transfer occurs between BSA and CPL. According to the binding parameters and ΔG(0)= negative values and ΔS(0)= 28.275 j mol(-1)K(-1), a static quenching process is effective in the CPL-BSA interaction spontaneously. ΔG(0) for the CPL-BSA complex obtained from the docking simulation is -28.99 kj mol(-1), which is close to experimental ΔG of binding, -21.349 kj mol(-1) that indicates a good agreement between the results of docking methods and experimental data. Conclusion: The outcomes of spectroscopic methods revealed that the conformation of BSA changed during drug-BSA interaction. The results of FRET propose that CPL quenches the fluorescence of BSA by static quenching and FRET. The displacement study showed that phenylbutazon and ketoprofen displaced CPL, indicating that its binding site on albumin is site I and Gentamicin cannot be displaced from the binding site of CPL. All results of molecular docking method agreed with the results of experimental data. Tabriz University of Medical Sciences 2016 2016-09-28 /pmc/articles/PMC5108985/ /pubmed/27853676 http://dx.doi.org/10.15171/bi.2016.19 Text en © 2016 The Author(s) This work is published by BioImpacts as an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by-nc/4.0/). Non-commercial uses of the work are permitted, provided the original work is properly cited.
spellingShingle Original Article
Hamishehkar, Hamed
Hosseini, Soheila
Naseri, Abdolhossein
Safarnejad, Azam
Rasoulzadeh, Farzaneh
Interactions of cephalexin with bovine serum albumin: displacement reaction and molecular docking
title Interactions of cephalexin with bovine serum albumin: displacement reaction and molecular docking
title_full Interactions of cephalexin with bovine serum albumin: displacement reaction and molecular docking
title_fullStr Interactions of cephalexin with bovine serum albumin: displacement reaction and molecular docking
title_full_unstemmed Interactions of cephalexin with bovine serum albumin: displacement reaction and molecular docking
title_short Interactions of cephalexin with bovine serum albumin: displacement reaction and molecular docking
title_sort interactions of cephalexin with bovine serum albumin: displacement reaction and molecular docking
topic Original Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5108985/
https://www.ncbi.nlm.nih.gov/pubmed/27853676
http://dx.doi.org/10.15171/bi.2016.19
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