Study of Interaction between Febuxostat and Bovine Serum Albumin by Fluorescence Spectroscopy
- *Corresponding Author:
- Md. Zakir Sultan
Centre for Advanced Research in Sciences
University of Dhaka, Dhaka 1000, Bangladesh
Tel: +880 296 619 20-59, Extn 4722
Fax: +880 2966 7222
E-mail: [email protected]
Received Date: July 12, 2015 Accepted Date: September 22, 2015 Published Date: September 25, 2015
Citation: Rabbi SNI, Sultan MdZ, Sohel MdD, Sultan MdZ (2015) Study of Interaction between Febuxostat and Bovine Serum Albumin by Fluorescence Spectroscopy. J Bioanal Biomed 07:164-170. doi:10.4172/1948-593X.1000138
Copyright: © 2015 Rabbi SNI, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
The interaction of an anti-gout drug, febuxostat was studied with bovine serum albumin (BSA) applying fluorescence quenching method for the first time. Interaction parameter and magnitude of the force indicated for both, dynamic and static quenching in between febuxostat and BSA protein. Thermodynamic studies indicated for both hydrogen and hydrophobic interactions, observed at 280 nm and only hydrophobic at 293 nm excitation wavelength. Negative ΔHo and positive ΔSo, indicated for distinctive characteristics for the existence of both, hydrogen and hydrophobic binding throughout the interactions. The binding constant Kb at λex=280 nm was 3.467 × 103 μM-1 and 4.943 × 103 μM-1 at 298 and 308 K temperature whereas, 5.54 × 103 μM-1 and 4.44 × 103 μM-1 was noted during excitation at λex=293 nm wavelength. The Kb values in different temperatures assumed that the stability of binding increased with the increase of temperature at λex=280 nm, but reverse effect was experienced at an excitation wavelength of λex=293 nm. The number of bound febuxostat molecules per BSA protein was found ~1.5 at both 298 and 308 K.