Journal of Bioanalysis & Biomedicine

Study of Interaction between Febuxostat and Bovine Serum Albumin by Fluorescence Spectroscopy

Abstract

Sikder Nahidul Islam Rabbi, Md. Zamil Sultan, Md. Didaruzzaman Sohel and Md. Zakir Sultan

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 ΔS_o, indicated for distinctive characteristics for the existence of both, hydrogen and hydrophobic binding throughout the interactions. The binding constant K_b at λ_ex=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 λ_ex=293 nm wavelength. The K_b values in different temperatures assumed that the stability of binding increased with the increase of temperature at λ_ex=280 nm, but reverse effect was experienced at an excitation wavelength of λ_ex=293 nm. The number of bound febuxostat molecules per BSA protein was found ~1.5 at both 298 and 308 K.