Molecular Modeling and Docking of Aquaporin Inhibitors to Reveal New Insights into Schistosomiasis Treatment.

BACKGROUND

Schistosomiasis (snail fever/bilharzia), a disease caused by parasitic flatworms (schistosomes), infects millions of people worldwide. Aquaporins from these organisms were found to be a potent drug target.

INTRODUCTION

We investigate the possible mechanism of inhibition of Aquaporin (AQP) from S.mansoni by 5 drug molecules (Praziquantel, Metrifonate, Artimisinin, Albendazole, and Amoscanate).

METHODS

3D molecular structure of Aquaporin was obtained through homology modeling and further protein-ligand docking and MD simulation were performed.

RESULTS

VAL-75, ASN-91, ALA-220, ASN-222, ARG-225 amino acids were found to play crucial role in ligand binding. TRP-71 and other important residues play major role in hydrophobic interactions stabilizing protein-ligand complexes.

CONCLUSION

We hope that this study (with the newly identified aquaporin target) will support the development of structure and pharmacophore-based novel S. mansoni drugs to control and curb Schistosomiasis.