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Indian Journal of Pharmaceutical Education and ResearchNOW IN
Article

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

Aimi Nabila Mohamad Saufi1, Nor Farrah Wahidah Ridzwan2, Saharuddin Bin Mohamad2,3, Saad Tayyab1,3, Adyani Azizah Abd Halim4★★ Corresponding author

  1. 1Biomolecular Research Group, Biochemistry Programme, Institute of Biological Sciences, Faculty of Science, University of Malaya, Kuala Lumpur, MALAYSIA.
  2. 2Bioinformatics Programme, Institute of Biological Sciences, Faculty of Science, University of Malaya, Kuala Lumpur, MALAYSIA.
  3. 3Centre of Research for Computational Sciences and Informatics for Biology, Bioindustry, Environment, Agriculture and Healthcare, University of Malaya, Kuala Lumpur, MALAYSIA.
  4. 4Department of Oral and Craniofacial Sciences, Faculty of Dentistry, University of Malaya, Kuala Lumpur, MALAYSIA.

CORRESPONDENCE

Adyani Azizah Abd Halim

Department of Oral and Craniofacial Sciences, Faculty of Dentistry, University of Malaya, Kuala Lumpur, MALAYSIA.

adyaniazizah@um.edu.my

Received: 04-03-2019; Revised: 26-04-2019; Accepted: 26-07-2019.

Volume 53, Issue 4 · pp. 682–687 · PUBLISHED 2019 · DOI: 10.5530/ijper.53.4.131

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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.

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    Saufi, A. N. M., Ridzwan, N. F. W., Mohamad, S. B., Tayyab, S., & Halim, A. A. A. (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), 682–687. https://doi.org/10.5530/ijper.53.4.131