Effects of interaction between non-steroidal anti-inflammatory drugs with BSA and DNA base Spectral, electrochemical and molecular docking methods

Main Authors: N. Rajendiran, J. Thulasidhasan
Format: Article Journal
Bahasa: eng
Terbitan: , 2017
Subjects:
BSA
Online Access: https://zenodo.org/record/5604319
ctrlnum 5604319
fullrecord <?xml version="1.0"?> <dc schemaLocation="http://www.openarchives.org/OAI/2.0/oai_dc/ http://www.openarchives.org/OAI/2.0/oai_dc.xsd"><creator>N. Rajendiran</creator><creator>J. Thulasidhasan</creator><date>2017-01-01</date><description>Department of Chemistry, Annamalai University, Annamalai Nagar-608 002, Tamilnadu, India E-mail : drrajendiran@rediffmail.com Manuscript received online 09 April 2016, accepted 03 October 2016 To evaluate the role of hydrophobic and electrostatic interactions of BSA and DNA base (adenine) with two different non-steroidal anti-inflammatory drugs, [meloxicam (MEX) and piroxicam (PIR)]. Both drugs have different heterocyclic rings. The binding affinity for the protein-drug formation is found to depend primarily on the different heterocyclic rings or functional groups like OH, C=O, NH, etc. suggesting the essential role of hydrophobic forces, supported by hydrogen and polar bonding interactions at the protein surface. UV-Visible, fluorescence, IR, cyclic voltammetry and molecular docking analysis were performed to compare the effects of heterocyclic rings of two drugs on BSA/adenine. The fluorescence spectral blue shift suggested that both drug molecules strongly interacted with BSA. The difference in the IR spectrum of BSA, pure drugs and complex confirm the interactions between the drugs to BSA. With an increase the concentration of drugs, the oxidation peaks of MEX and PIR were shifted to higher potential (Epa) and the oxidation peak current (Ipa) is also increased. These observations suggested the formation of non-electroactive interactions between BSA/adenine with drug molecules. Docking analysis showed PIR strongly interacted with BSA rather than MEX</description><identifier>https://zenodo.org/record/5604319</identifier><identifier>10.5281/zenodo.5604319</identifier><identifier>oai:zenodo.org:5604319</identifier><language>eng</language><relation>doi:10.5281/zenodo.5604318</relation><rights>info:eu-repo/semantics/openAccess</rights><rights>https://creativecommons.org/licenses/by/4.0/legalcode</rights><source>Journal of Indian Chemical Society Vol. 94(Jan-2017) 83-93</source><subject>BSA</subject><subject>meloxicam</subject><subject>piroxicam</subject><subject>fluorescence quenching</subject><subject>cyclic voltammetry</subject><subject>molecular docking</subject><title>Effects of interaction between non-steroidal anti-inflammatory drugs with BSA and DNA base : Spectral, electrochemical and molecular docking methods</title><type>Journal:Article</type><type>Journal:Article</type><recordID>5604319</recordID></dc>
language eng
format Journal:Article
Journal
Journal:Journal
author N. Rajendiran
J. Thulasidhasan
title Effects of interaction between non-steroidal anti-inflammatory drugs with BSA and DNA base : Spectral, electrochemical and molecular docking methods
title_sub Spectral, electrochemical and molecular docking methods
publishDate 2017
topic BSA
meloxicam
piroxicam
fluorescence quenching
cyclic voltammetry
molecular docking
url https://zenodo.org/record/5604319
contents Department of Chemistry, Annamalai University, Annamalai Nagar-608 002, Tamilnadu, India E-mail : drrajendiran@rediffmail.com Manuscript received online 09 April 2016, accepted 03 October 2016 To evaluate the role of hydrophobic and electrostatic interactions of BSA and DNA base (adenine) with two different non-steroidal anti-inflammatory drugs, [meloxicam (MEX) and piroxicam (PIR)]. Both drugs have different heterocyclic rings. The binding affinity for the protein-drug formation is found to depend primarily on the different heterocyclic rings or functional groups like OH, C=O, NH, etc. suggesting the essential role of hydrophobic forces, supported by hydrogen and polar bonding interactions at the protein surface. UV-Visible, fluorescence, IR, cyclic voltammetry and molecular docking analysis were performed to compare the effects of heterocyclic rings of two drugs on BSA/adenine. The fluorescence spectral blue shift suggested that both drug molecules strongly interacted with BSA. The difference in the IR spectrum of BSA, pure drugs and complex confirm the interactions between the drugs to BSA. With an increase the concentration of drugs, the oxidation peaks of MEX and PIR were shifted to higher potential (Epa) and the oxidation peak current (Ipa) is also increased. These observations suggested the formation of non-electroactive interactions between BSA/adenine with drug molecules. Docking analysis showed PIR strongly interacted with BSA rather than MEX
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