Combination mode of antimalarial drug mefloquine and human serum albumin: Insights from spectroscopic and docking approaches
The interaction between mefloquine (MEF), the antimalarial drug, and human serum albumin (HSA), the main carrier protein in blood circulation, was explored using fluorescence, absorption, and circular dichroism spectroscopic techniques. Quenching of HSA fluorescence with MEF was characterized as sta...
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my.um.eprints.372462023-03-09T02:06:26Z http://eprints.um.edu.my/37246/ Combination mode of antimalarial drug mefloquine and human serum albumin: Insights from spectroscopic and docking approaches Musa, Kabiru A. Ridzwan, Nor F. W. Mohamad, Saharuddin Tayyab, Saad QH301 Biology The interaction between mefloquine (MEF), the antimalarial drug, and human serum albumin (HSA), the main carrier protein in blood circulation, was explored using fluorescence, absorption, and circular dichroism spectroscopic techniques. Quenching of HSA fluorescence with MEF was characterized as static quenching and thus confirmed the complex formation between MEF and HSA. Association constant values for MEF-HSA interaction were found to fall within the range of 3.79-5.73 x 10(4) M-1 at various temperatures (288, 298, and 308 K), which revealed moderate binding affinity. Hydrogen bonds and hydrophobic interactions were predicted to connect MEF and HSA together in the MEF-HSA complex, as deduced from the thermodynamic data (Delta S = +133.52 J mol(-1) K-1 and Delta H = +13.09 kJ mol(-1)) of the binding reaction and molecular docking analysis. Three-dimensional fluorescence spectral analysis pointed out alterations in the microenvironment around aromatic amino acid (tryptophan and tyrosine) residues of HSA consequent to the addition of MEF. Circular dichroic spectra of HSA in the wavelength ranges of 200-250 and 250-300 nm hinted smaller changes in the protein's secondary and tertiary structures, respectively, induced by MEF binding. Noncovalent conjugation of MEF to HSA bettered protein thermostability. Site marker competitive drug displacement results suggested HSA Sudlow's site I as the MEF binding site, which was also supported by molecular docking analysis. Wiley 2020-02 Article PeerReviewed Musa, Kabiru A. and Ridzwan, Nor F. W. and Mohamad, Saharuddin and Tayyab, Saad (2020) Combination mode of antimalarial drug mefloquine and human serum albumin: Insights from spectroscopic and docking approaches. Biopolymers, 111 (2). ISSN 0006-3525, DOI https://doi.org/10.1002/bip.23337 <https://doi.org/10.1002/bip.23337>. 10.1002/bip.23337 |
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QH301 Biology Musa, Kabiru A. Ridzwan, Nor F. W. Mohamad, Saharuddin Tayyab, Saad Combination mode of antimalarial drug mefloquine and human serum albumin: Insights from spectroscopic and docking approaches |
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The interaction between mefloquine (MEF), the antimalarial drug, and human serum albumin (HSA), the main carrier protein in blood circulation, was explored using fluorescence, absorption, and circular dichroism spectroscopic techniques. Quenching of HSA fluorescence with MEF was characterized as static quenching and thus confirmed the complex formation between MEF and HSA. Association constant values for MEF-HSA interaction were found to fall within the range of 3.79-5.73 x 10(4) M-1 at various temperatures (288, 298, and 308 K), which revealed moderate binding affinity. Hydrogen bonds and hydrophobic interactions were predicted to connect MEF and HSA together in the MEF-HSA complex, as deduced from the thermodynamic data (Delta S = +133.52 J mol(-1) K-1 and Delta H = +13.09 kJ mol(-1)) of the binding reaction and molecular docking analysis. Three-dimensional fluorescence spectral analysis pointed out alterations in the microenvironment around aromatic amino acid (tryptophan and tyrosine) residues of HSA consequent to the addition of MEF. Circular dichroic spectra of HSA in the wavelength ranges of 200-250 and 250-300 nm hinted smaller changes in the protein's secondary and tertiary structures, respectively, induced by MEF binding. Noncovalent conjugation of MEF to HSA bettered protein thermostability. Site marker competitive drug displacement results suggested HSA Sudlow's site I as the MEF binding site, which was also supported by molecular docking analysis. |
format |
Article |
author |
Musa, Kabiru A. Ridzwan, Nor F. W. Mohamad, Saharuddin Tayyab, Saad |
author_facet |
Musa, Kabiru A. Ridzwan, Nor F. W. Mohamad, Saharuddin Tayyab, Saad |
author_sort |
Musa, Kabiru A. |
title |
Combination mode of antimalarial drug mefloquine and human serum albumin: Insights from spectroscopic and docking approaches |
title_short |
Combination mode of antimalarial drug mefloquine and human serum albumin: Insights from spectroscopic and docking approaches |
title_full |
Combination mode of antimalarial drug mefloquine and human serum albumin: Insights from spectroscopic and docking approaches |
title_fullStr |
Combination mode of antimalarial drug mefloquine and human serum albumin: Insights from spectroscopic and docking approaches |
title_full_unstemmed |
Combination mode of antimalarial drug mefloquine and human serum albumin: Insights from spectroscopic and docking approaches |
title_sort |
combination mode of antimalarial drug mefloquine and human serum albumin: insights from spectroscopic and docking approaches |
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Wiley |
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2020 |
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http://eprints.um.edu.my/37246/ |
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1761616813971472384 |
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13.18916 |