Fluorometric and Docking Analysis of the Complex Formation between an Anti-Cancer Drug, Chlorambucil and Bovine Serum Albumin

Saufi, Aimi Nabila Mohamad and Ridzwan, Nor Farrah Wahidah and Mohamad, Saharuddin and Tayyab, Saad and Abd Halim, Adyani Azizah (2019) Fluorometric and Docking Analysis of the Complex Formation between an Anti-Cancer Drug, Chlorambucil and Bovine Serum Albumin. Indian Journal of Pharmaceutical Education and Research, 53 (4). pp. 682-687. ISSN 0019-5464

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Official URL: https://doi.org/10.5530/ijper.53.4.131

Abstract

Background: To characterize the interaction between chlorambucil (CHB) and the carrier protein, bovine serum albumin (BSA) in order to understand the transport of this drug in blood circulation. Methods: Fluorescence quenching titration method was used to examine the interaction of CHB with BSA by determining its binding constant and binding stoichiometry. The binding site identification was probed with molecular docking techniques. Results: Values of the Stern-Volmer constant (KSV), bimolecular quenching rate constant (kq)and binding constant (K) for CHB-BSA system were determined a as 3.57×104 M−1, 5.67 × 1012 M−1 s−1 and 5.58 × 104 M−1, respectively. Binding stoichiometry was found to be ~1.0, as obtained from the double logarithmic plot. The molecular docking results revealed that CHB binds to both Site I and Site II of BSA, however Site II was predicted to be the preferred binding site. Conclusion: The value of Ka suggested intermediate binding affinity between CHB and BSA with the binding stoichiometry of 1:1. CHB was found to have the binding preference at Site II of BSA due to formation of greater contacts. © 2019, Association of Pharmaceutical Teachers of India. All rights reserved.

Item Type: Article
Uncontrolled Keywords: Bovine serum albumin; Chlorambucil; Drug-protein interaction; Fluorescence quenching; Molecular docking
Subjects: Q Science > Q Science (General)
Q Science > QH Natural history
Q Science > QR Microbiology
Divisions: Faculty of Dentistry
Faculty of Science > Institute of Biological Sciences
Depositing User: Ms. Juhaida Abd Rahim
Date Deposited: 21 Jan 2020 07:35
Last Modified: 21 Jan 2020 07:35
URI: http://eprints.um.edu.my/id/eprint/23512

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