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<p><i>Trichinella spiralis</i> is a nematode parasite, the common cause of human disease. Trichinellosis: the infection occurs after the consumption of raw or undercooked pork meat. In many parasitic helminths, cysteine proteases are the principal source of amino acids. In <i>Trichinella spiralis</i>, cathepsin B cysteine proteases contribute to the parasite penetration into the host’s gut wall, moulting, feeding, immune escaping, and degradation of haemoglobin. Basically, cathepsin B cysteine proteases are known for its proteolytic activities and it can degrade the host intestinal epithelial cell junctions and enable parasite entry during the early stages of infection. The aim of this study is to characterise and inhibit the synthesis of cathepsin B cysteine proteases by using natural product as inhibitors of protein to control the population of nematode parasite in human host. In the ExPASy server ProtParam tool were used to perform the cysteine protease cathepsin B physicochemical analysis. In secondary structure analysis amino acid composition of cathepsin B protein were predicted by PredictProtein. Based on availability, ADME properties analysis and binding affinities of all the studied phytochemicals, the molecules Panduratin A, Nicolaioidesin C, Guttiferone A, and Garciniaphenone, shows drugability. The AutoDock automated docking tool were used for molecular docking analysis and predicting the optimal protein–ligand interactions between the cathepsin B and Panduratin A, Nicolaioidesin C, Guttiferone A, and Garciniaphenone. In silico analysis of Cathepsin B (329 amino acids) shows that it is quite stable protein with Aliphatic index 65.84 and composed of helix is 15.81%, strand 17.02% and other part is 67.17%. The molecular docking analysis results revealed that amongst the studies ligands Panduratin A and Nicolaioidesin C, shows the similar affinity towards protein i.e. (− 7.5&#xa0;kcal/mol) with formation of 2 and 3 hydrogen bond interactions respectively, While Guttiferone A (− 7.4&#xa0;kcal/mol) 4 hydrogen bond interactions and Garciniaphenone (− 7.2&#xa0;kcal/mol) 3 hydrogen bond interactions. The small molecule as inhibitors and understanding their utility as vaccine candidate against nematodes is recent active area of research. These results indicates that the cathepsin B which is the key contributors to the digestion of host proteins of the <i>Trichinella spiralis</i> parasite may be a good candidate to design the synthetic drug against the nematode infections.</p>

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Characterisations and molecular docking of cathepsin B cysteine proteinase a novel drug target for parasitic nematode Trichinella spiralis

  • 期刊论文

  • 发表日期：

    2026年2月20日

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  • Somnath Waghmare,
  • Anil Kumar,
  • Balde Govind

摘要

Trichinella spiralis is a nematode parasite, the common cause of human disease. Trichinellosis: the infection occurs after the consumption of raw or undercooked pork meat. In many parasitic helminths, cysteine proteases are the principal source of amino acids. In Trichinella spiralis, cathepsin B cysteine proteases contribute to the parasite penetration into the host’s gut wall, moulting, feeding, immune escaping, and degradation of haemoglobin. Basically, cathepsin B cysteine proteases are known for its proteolytic activities and it can degrade the host intestinal epithelial cell junctions and enable parasite entry during the early stages of infection. The aim of this study is to characterise and inhibit the synthesis of cathepsin B cysteine proteases by using natural product as inhibitors of protein to control the population of nematode parasite in human host. In the ExPASy server ProtParam tool were used to perform the cysteine protease cathepsin B physicochemical analysis. In secondary structure analysis amino acid composition of cathepsin B protein were predicted by PredictProtein. Based on availability, ADME properties analysis and binding affinities of all the studied phytochemicals, the molecules Panduratin A, Nicolaioidesin C, Guttiferone A, and Garciniaphenone, shows drugability. The AutoDock automated docking tool were used for molecular docking analysis and predicting the optimal protein–ligand interactions between the cathepsin B and Panduratin A, Nicolaioidesin C, Guttiferone A, and Garciniaphenone. In silico analysis of Cathepsin B (329 amino acids) shows that it is quite stable protein with Aliphatic index 65.84 and composed of helix is 15.81%, strand 17.02% and other part is 67.17%. The molecular docking analysis results revealed that amongst the studies ligands Panduratin A and Nicolaioidesin C, shows the similar affinity towards protein i.e. (− 7.5 kcal/mol) with formation of 2 and 3 hydrogen bond interactions respectively, While Guttiferone A (− 7.4 kcal/mol) 4 hydrogen bond interactions and Garciniaphenone (− 7.2 kcal/mol) 3 hydrogen bond interactions. The small molecule as inhibitors and understanding their utility as vaccine candidate against nematodes is recent active area of research. These results indicates that the cathepsin B which is the key contributors to the digestion of host proteins of the Trichinella spiralis parasite may be a good candidate to design the synthetic drug against the nematode infections.