Exploring the interaction between the antiallergic drug, tranilast and human serum albumin: Insights from calorimetric, spectroscopic and modeling studies

Tayyab, S. and Zaroog, M.S. and Feroz, S.R. and Mohamad, S.B. and Malek, S.N.A. (2015) Exploring the interaction between the antiallergic drug, tranilast and human serum albumin: Insights from calorimetric, spectroscopic and modeling studies. International Journal of Pharmaceutics, 491 (1-2). pp. 352-358. ISSN 0378-5173

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Official URL: http://dx.doi.org/10.1016/j.ijpharm.2015.06.042

Abstract

The interaction of tranilast (TRN), an antiallergic drug with the main drug transporter in human circulation, human serum albumin (HSA) was studied using isothermal titration calorimetry (ITC), fluorescence spectroscopy and in silico docking methods. ITC data revealed the binding constant and stoichiometry of binding as (3.21 ± 0.23) × 106 M-1 and 0.80 ± 0.08, respectively, at 25 °C. The values of the standard enthalpy change (ΔH°) and the standard entropy change (ΔS°) for the interaction were found as -25.2 ± 5.1 kJ mol-1 and 46.9 ± 5.4 J mol-1 K-1, respectively. Both thermodynamic data and modeling results suggested the involvement of hydrogen bonding, hydrophobic and van der Waals forces in the complex formation. Three-dimensional fluorescence data of TRN-HSA complex demonstrated significant changes in the microenvironment around the protein fluorophores upon drug binding. Competitive drug displacement results as well as modeling data concluded the preferred binding site of TRN as Sudlow's site I on HSA.

Item Type: Article
Uncontrolled Keywords: Tranilast; Human serum albumin; Isothermal titration calorimetry; Ligand binding; Molecular docking
Subjects: Q Science > Q Science (General)
Q Science > QH Natural history
Divisions: Faculty of Science > Institute of Biological Sciences
Depositing User: Ms. Juhaida Abd Rahim
Date Deposited: 03 Oct 2018 08:37
Last Modified: 03 Oct 2018 08:37
URI: http://eprints.um.edu.my/id/eprint/19579

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