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Appl. Sci. 2017, 7(6), 617; doi:10.3390/app7060617

Synthesis and Biophysical Insights into the Binding of a Potent Anti-Proliferative Non-symmetric Bis-isatin Derivative with Bovine Serum Albumin: Spectroscopic and Molecular Docking Approaches

1
Department of Pharmaceutical Chemistry, College of Pharmacy, King Saud University, P.O. Box 2457, Riyadh 11451, Saudi Arabia
2
Department of Pharmaceutical Chemistry, Faculty of Pharmacy, Kafrelsheikh University, Kafrelsheikh 33516, Egypt
3
Department of Applied Organic Chemistry, National Research Centre, Dokki, Giza 12622, Egypt
4
Medicinal and Pharmaceutical Chemistry Department, Pharmaceutical and Drug Industries Research Division, National Research Centre, Dokki, Giza 12622, Egypt
*
Authors to whom correspondence should be addressed.
Academic Editor: Helmut Martin Hügel
Received: 21 May 2017 / Revised: 11 June 2017 / Accepted: 12 June 2017 / Published: 14 June 2017
(This article belongs to the Section Chemistry)
View Full-Text   |   Download PDF [5945 KB, uploaded 16 June 2017]   |  

Abstract

As part of the research endeavors to combat cancer, a non-symmetric bis-isatin derivative (compound 3) was synthesized and showed a significant anti-proliferative potency. The current study provides a comprehensive characterization of the interaction of compound 3 with the drug-transporting protein bovine serum albumin (BSA) via the use of spectroscopic tools along with molecular docking studies. Fluorescence spectral measurements showed that the BSA intrinsic fluorescence can be significantly quenched by the addition of compound 3 and the formation of a non-fluorescent complex. Further measurements revealed a static type of quenching with Stern–Volmer and Linweaver–Burk constants of 105. The thermodynamic parameters of the binding were calculated to be ΔS° 105.09 ± 5.32 with ΔH° of −0.72 ± 0.71 and negative ΔG° values. In addition, synchronous fluorescence and 3D fluorescence spectroscopy suggested that compound 3 did not induce conformational changes in BSA. Site competition experiments revealed that compound 3 competes with warfarin within the BSA binding domain (Sudlow site I). This was further confirmed by the molecular docking results showing a binding energy of −25.93 kJ/mol for compound 3-BSA. Hence, the observed results in the present study assumed that the compound 3-BSA binding is spontaneous, involving electrostatic forces and hydrogen bonding. View Full-Text
Keywords: fluorescence spectroscopy; bovine serum albumin; isatin derivatives; anti-proliferative agent fluorescence spectroscopy; bovine serum albumin; isatin derivatives; anti-proliferative agent
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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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Abdelhameed, A.S.; Bakheit, A.H.; Mohamed, M.S.; Eldehna, W.M.; Abdel-Aziz, H.A.; Attia, M.I. Synthesis and Biophysical Insights into the Binding of a Potent Anti-Proliferative Non-symmetric Bis-isatin Derivative with Bovine Serum Albumin: Spectroscopic and Molecular Docking Approaches. Appl. Sci. 2017, 7, 617.

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