Table of Contents
Journal of Biophysics
Volume 2014 (2014), Article ID 675905, 7 pages
http://dx.doi.org/10.1155/2014/675905
Research Article

Interaction between Gallotannin and a Recombinant Form of Arginine Kinase of Trypanosoma brucei: Thermodynamic and Spectrofluorimetric Evaluation

1Department of Biological Sciences, Landmark University, Omu-Aran 370102, Nigeria
2Department of Biochemistry, Faculty of Life Sciences, University of Ilorin, Ilorin 240001, Nigeria
3Department of Biochemistry, Ambrose Alli University, Ekpoma 310001, Nigeria

Received 17 June 2014; Revised 24 July 2014; Accepted 12 August 2014; Published 26 August 2014

Academic Editor: Rizwan Hasan Khan

Copyright © 2014 O. S. Adeyemi et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

Current chemotherapies against trypanosomiasis are beset with diverse challenges, a situation which underscores the numerous research efforts aimed at finding newer and effective treatments. Arginine kinase of trypanosome has been validated as target for drug development against trypanosomiasis. The present study investigated the interaction between a recombinant form of the arginine kinase (rTbAK) of trypanosome and gallotannin. The interaction between gallotannin and recombinant arginine kinase of Trypanosoma brucei caused significant decrease of enzyme activity. Kinetic analysis revealed the interaction to be of noncompetitive inhibition. Further thermodynamic analysis showed that the interaction between gallotannin and the recombinant arginine kinase was nonspontaneous and involved hydrophobic forces. The values and the FRET analysis suggest that static quenching of fluorescence intensity by gallotannin was static. Data revealed inhibitory interactions between gallotannin and rTbAK of trypanosome. Although the mechanism of inhibition is not clear yet, molecular docking studies are ongoing to clearly define the inhibitory interactions between the gallotannin and rTbAK. The knowledge of such binding properties would enrich development of selective inhibitors for the arginine kinase of Trypanosoma brucei.