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

  • Aimi Nabila Mohamad Saufi1Biomolecular Research Group, Biochemistry Programme, Institute of Biological Sciences, Faculty of Science, University of Malaya, Kuala Lumpur, MALAYSIA.
  • Nor Farrah Wahidah Ridzwan2Bioinformatics Programme, Institute of Biological Sciences, Faculty of Science, University of Malaya, Kuala Lumpur, MALAYSIA.
  • Saharuddin Bin Mohamad2Bioinformatics Programme, Institute of Biological Sciences, Faculty of Science, University of Malaya, Kuala Lumpur, MALAYSIA., 3Centre of Research for Computational Sciences and Informatics for Biology, Bioindustry, Environment, Agriculture and Healthcare, University of Malaya, Kuala Lumpur, MALAYSIA.
  • Saad Tayyab1Biomolecular Research Group, Biochemistry Programme, Institute of Biological Sciences, Faculty of Science, University of Malaya, Kuala Lumpur, MALAYSIA., 3Centre of Research for Computational Sciences and Informatics for Biology, Bioindustry, Environment, Agriculture and Healthcare, University of Malaya, Kuala Lumpur, MALAYSIA.
  • Adyani Azizah Abd Halim4Department of Oral and Craniofacial Sciences, Faculty of Dentistry, University of Malaya, Kuala Lumpur, MALAYSIA.

Volume 53 Issue 4 Pages 682-687

DOI: 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 (Ka) for CHB-BSA system were determined 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.

Keywords

  • Bovine serum albumin
  • Chlorambucil
  • Drug-protein interaction
  • Fluorescence
  • quenching
  • Molecular docking
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