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.

背景：血吸虫病（蜗牛热/血吸虫病）是一种由寄生扁虫（血吸虫）引起的疾病，全世界有数百万人感染。发现来自这些生物体的水通道蛋白是一种有效的药物靶点。

简介：我们研究了 5 种药物分子（吡喹酮、甲磺草酸、青蒿素、阿苯达唑和阿莫斯卡酸盐）抑制曼氏链球菌水通道蛋白 (AQP) 的可能机制。

方法：通过同源建模获得水通道蛋白的3D分子结构，并进一步进行蛋白质-配体对接和MD模拟。

结果：发现 VAL-75、ASN-91、ALA-220、ASN-222、ARG-225 氨基酸在配体结合中起关键作用。TRP-71 和其他重要的残基在稳定蛋白质-配体复合物的疏水相互作用中起主要作用。

结论：我们希望这项研究（使用新确定的水通道蛋白靶点）将支持开发基于结构和药效团的新型曼氏链球菌药物，以控制和遏制血吸虫病。