Structure-based virtual screening of β-tubulin and thioredoxin reductase in Brugia malayi: a step toward novel anti-filarial agents

基于结构的马来丝虫β-微管蛋白和硫氧还蛋白还原酶虚拟筛选:迈向新型抗丝虫药物的一步

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Abstract

BACKGROUND: Lymphatic filariasis, or elephantiasis, is a neglected tropical disease caused by filarial nematodes such as Brugia malayi. Current antifilarial drugs-diethylcarbamazine (DEC), albendazole, and ivermectin form the basis of mass drug administration (MDA) programs for lymphatic filariasis. While effective against microfilarial stages, these agents show little or no macrofilaricidal activity, necessitating repeated treatment rounds to interrupt transmission. Growing evidence of reduced efficacy and emerging resistance further threatens the sustainability of these regimens. Thioredoxin reductase (TrxR) and β-tubulin are critical for parasite survival: TrxR maintains redox balance and protects against oxidative stress, while β-tubulin supports cytoskeletal integrity, intracellular transport, and cell division. Their combined roles in stress adaptation and structural stability make them compelling dual targets. This study employed structure-based virtual screening, molecular docking, and molecular dynamics simulations (MDS) to identify novel thiol-based inhibitors against both proteins. RESULTS: A total of 467 compounds were virtually screened, leading to the identification of seven lead candidates with superior docking scores (- 8.5 to - 4.0 kcal/mol) compared to the standard drug albendazole (- 5.3 to - 4.5 kcal/mol). Notably, compound 15 demonstrated the strongest binding affinity coupled with an optimal toxicity profile. Pharmacokinetic analysis using ADME assays confirmed drug-likeness and oral bioavailability of the top ligands, with minimal Lipinski's rule violations. Molecular dynamics simulations exceeding 100 ns revealed sustained stability of the protein-ligand complex, which was further supported by RMSD and RMSF analyses, demonstrating conformational stability. Principal interactions comprised hydrogen bonding, hydrophobic contacts, and π-stacking with conserved residues within the active sites of the target proteins. CONCLUSION: The integrated in silico approach combining docking, pharmacokinetic profiling, and MDS successfully identified potent thiol-based ligands with high affinity for β-tubulin and TrxR in B. malayi. Among these, HI/CYR/TH-15 emerged as the most promising lead. These findings provide a foundation for the development of next-generation anti-filarial therapies targeting multiple life stages, warranting further in vitro and in vivo validation to confirm therapeutic potential. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1007/s40203-025-00474-7.

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