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Please use this identifier to cite or link to this item: http://repository.li.mahidol.ac.th/dspace/handle/123456789/49543
Title: Insight into the molecular interaction of cloxyquin (5-chloro-8-hydroxyquinoline) with bovine serum albumin: Biophysical analysis and computational simulation
Authors: Kamonrat Phopin
Waralee Ruankham
Supaluk Prachayasittikul
Virapong Prachayasittikul
Tanawut Tantimongcolwat
Mahidol University
Keywords: Biochemistry, Genetics and Molecular Biology;Chemical Engineering;Chemistry;Computer Science
Issue Date: 1-Jan-2020
Citation: International Journal of Molecular Sciences. Vol.21, No.1 (2020)
Abstract: © 2019 by the authors. Licensee MDPI, Basel, Switzerland. Cloxyquin is a potential therapeutic compound possessing various bioactivities, especially antibacterial, antifungal, cardioprotective, and pain relief activities. Herein, the interaction mechanism between cloxyquin and bovine serum albumin (BSA) has been elucidated in order to fulfill its pharmacokinetic and pharmacodynamic gaps essential for further development as a therapeutic drug. Multi-spectroscopic and biophysical model analysis suggested that cloxyquin interacts with BSA via a static process by ground-state complex formation. Its binding behavior emerged as a biphasic fashion with a moderate binding constant at the level of 104 M−1. Thermodynamic analysis and molecular docking simulation concurrently revealed that hydrophobic interaction is a major driving force for BSA–cloxyquin complexation. Binding of cloxyquin tends to slightly enlarge the monomeric size of BSA without a significant increase of aggregate fraction. Cloxyquin preferentially binds into the fatty acid binding site 5 (FA5) of the BSA via hydrophobic interaction amongst its quinoline scaffold and Phe550, Leu531, and Leu574 residues of BSA. The quinoline ring and hydroxyl moiety of cloxyquin also form the π–π interaction and the hydrogen bond with Phe506. Our data indicate a potential function of serum albumin as a carrier of cloxyquin in blood circulation.
URI: http://repository.li.mahidol.ac.th/dspace/handle/123456789/49543
metadata.dc.identifier.url: https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85077529056&origin=inward
ISSN: 14220067
16616596
Appears in Collections:Scopus 2020

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