Interaction of eugenol with xanthine oxidase: Multi spectroscopic and in silico modelling approach

Eugenol, a major component in clove has various biological activities. The current study focused to the binding potential of eugenol with Xanthine oxidase (XO) were evaluated using multi spectroscopic techniques and in silico docking studies. Xanthine oxidase, a superoxide generating enzyme, catalyses hypoxanthine and xanthine to uric acid. An excessive uric acid and superoxide anion radical in our body causes many serious clinical complications. The activity and the structural alterations can be a significant method to reduce this kind of risk factors. The results obtained from the fluorescence titration exhibited the interactions initiated by a static quenching mechanism. The ultraviolet (UV), fourier-transform infrared (FTIR), circular dichroism (CD) spectroscopic analysis of eugenol bind with XO indicated the secondary structural alteration in XO. Docking studies showed molecular level interaction of eugenol with the amino acid residues of Thr 1010, Phe 914, Phe 1009, Leu 1014, Phe 1009, Val 1011, Arg 880, Ala 1078, Glu 802, Leu 648and Leu 873 which residing at the catalytic active site of the XO. These results inferred that the eugenol can interact with XO in a remarkable manner and these findings provide a supporting data for the XO inhibition studies to propose a new lead compound.