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Published on:September 2019
Indian Journal of Pharmaceutical Education and Research, 2019; 53(4):682-687
Original Article | doi:10.5530/ijper.53.4.131

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


Authors and affiliation (s):

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

1Biomolecular Research Group, Biochemistry Programme, Institute of Biological Sciences, Faculty of Science, University of Malaya, Kuala Lumpur, MALAYSIA.

2Bioinformatics 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.

4Department of Oral and Craniofacial Sciences, Faculty of Dentistry, University of Malaya, Kuala Lumpur, MALAYSIA.

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. Material and 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 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 preference at site II of BSA due to formation of greater contacts.

Key words: Bovine serum albumin, Chlorambucil, Drug-protein interaction, Fluorescence quenching, Molecular docking.

 

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IJPER - An Official Publication of Association of Pharmaceutical Teachers of India is pleased to announce continued growth in the 2019 Release of Journal Citation Reports (source: 2018 Web of Science Data).

 

Impact Factor® as reported in the 2018 Journal Citation Reports® (Clarivate Analytics, 2019): 0.425

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The Official Journal of Association of Pharmaceutical Teachers of India (APTI)
(Registered under Registration of Societies Act XXI of 1860 No. 122 of 1966-1967, Lucknow)

Indian Journal of Pharmaceutical Education and Research (IJPER) [ISSN-0019-5464] is the official journal of Association of Pharmaceutical Teachers of India (APTI) and is being published since 1967.

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