ArticleOpen veterinary journal2024
Potency of anti-trematode in inhibiting cathepsin-2L and cathepsin-5L of
Article in Open veterinary journal, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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6 authors.
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Abstract
Background: Cathepsin-L (FhCL) is a group of enzymes that most flukes express and secreted significantly in parasite-host interactions. Researches are focusing on antigens released by Aim: This study was carried out to screen six commercial anthelmintic drugs against cathepsin-2L (FhCL-2) and cathepsin 5L (FhCL-5) using Methods: The three-dimensional (3D) crystal structure of FhCL-2 and FhCL-5 enzymes were constructed based on the crystal structure of ProCathepsin 1L (pdb id. 2O6X) as a template, while six anthelmintic agents ("SMILES" format) were downloaded from PubChem and converted to 3D format using the MOE Builder tool. The enzyme modeling results were evaluated using the "Ramachandran Plot". Results: Molecular docking results showed that all tested ligands had affinity for FhCL-2 and FhCL-5. The best ∆Gbinding value for FhCL-2 was clorsulon ligand (-15.21 kcal/mol) with pKi of 32.25 µM, which was significantly different compared to other drugs ( Conclusion: All of the tested anti-trematode ligands had potency as inhibitors for FhCL-2 and FhCL-5 enzymes of
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