Molecules 2017, 22(8), 1258; doi:10.3390/molecules22081258
Study of the Interactions of Bovine Serum Albumin with the New Anti-Inflammatory Agent 4-(1,3-Dioxo-1,3-dihydro-2H-isoindol-2-yl)-N′-[(4-ethoxy-phenyl)methylidene]benzohydrazide Using a Multi-Spectroscopic Approach and Molecular Docking
Tanveer A. Wani 1,*
, Ahmed H. Bakheit 1
, Abdul-Rahman A. Al-Majed 1, Mashooq A. Bhat 1 and Seema Zargar 2
, Abdul-Rahman A. Al-Majed 1, Mashooq A. Bhat 1 and Seema Zargar 21
Department of Pharmaceutical Chemistry, College of Pharmacy, King Saud University, P.O. Box 2457, Riyadh 11451, Saudi Arabia
2
Department of Biochemistry, College of Science, King Saud University, P.O. Box 22452, Riyadh 11451, Saudi Arabia
*
Author to whom correspondence should be addressed.
Received: 22 June 2017 / Revised: 15 July 2017 / Accepted: 26 July 2017 / Published: 27 July 2017
(This article belongs to the Special Issue Anti-inflammatory Agents)
Abstract
The lipophilic derivative of thalidomide (4-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)-N′-[(4-ethoxyphenyl)methylidene]benzohydrazide, 6P) was synthesized to enhance its characteristics and efficacy. Earlier studies have proved the immunomodulatory and anti-inflammatory effects of 6P. In this study the interaction between bovine serum albumin (BSA) and 6P was studied using a multi-spectroscopic approach which included UV spectrophotometry, spectrofluorimetry and three dimensional spectrofluorometric and molecular docking studies. Static quenching was involved in quenching the fluorescence of BSA by 6P, because a complex formation occurred between the 6P and BSA. The binding constant decreased with higher temperature and was in the range of 2.5 × 105–4.8 × 103 L mol−1 suggesting an unstable complex at higher temperatures. A single binding site was observed and the the site probe experiments showed site II (sub-domain IIIA) of BSA as the binding site for 6P. The negative values of ∆G0, ∆H0 and ∆S0 at (298/303/308 K) indicated spontaneous binding between 6P and BSA as well as the interaction was enthalpy driven and van der Waals forces and hydrogen bonding were involved in the interaction. The docking results and the results from the experimental studies are complimentary to each other and confirm that 6P binds at site II (sub-domain IIIA) of BSA. View Full-TextKeywords:
HSA; BSA; serum albumin; thalidomide; lipophilic thalidomide derivative; fluorescence; quenching; 6P
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).
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Wani, T.A.; Bakheit, A.H.; Al-Majed, A.-R.A.; Bhat, M.A.; Zargar, S. Study of the Interactions of Bovine Serum Albumin with the New Anti-Inflammatory Agent 4-(1,3-Dioxo-1,3-dihydro-2H-isoindol-2-yl)-N′-[(4-ethoxy-phenyl)methylidene]benzohydrazide Using a Multi-Spectroscopic Approach and Molecular Docking. Molecules 2017, 22, 1258.
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