ArticleDaru : journal of Faculty of Pharmacy, Tehran University of Medical Sciences2021
Molecular docking of alpha-enolase to elucidate the promising candidates against Streptococcus pneumoniae infection.
Article in Daru : journal of Faculty of Pharmacy, Tehran University of Medical Sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed, 19 citations in OpenAlex.
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- Osteoblast-Derived ECM1 Promotes Anti-Androgen Resistance in Bone Metastatic Prostate Cancer.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Identification of novel natural compounds against CFTR p.Gly628Arg pathogenic variant.AMB Express · 2024Article
- Pharmacological evaluation and phytochemical profiling of butanol extract of L. edodes with in- silico virtual screening.Scientific reports · 2024Article
- BeyondMolecular therapy oncolytics · 2023Review
- An alternative vaccine target for bovine Anaplasmosis based on enolase, a moonlighting protein.Frontiers in veterinary science · 2023Article
- Docking and Molecular Dynamics Study to Identify Novel Phytobiologics fromLife (Basel, Switzerland) · 2022Article
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Authors and funding
11 authors at 7 institutions in 5 countries.
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Abstract
purposeTo predict potential inhibitors of alpha-enolase to reduce plasminogen binding of Streptococcus pneumoniae (S. pneumoniae) that may lead as an orally active drug. S. pneumoniae remains dominant in causing invasive diseases. Fibrinolytic pathway is a critical factor of S. pneumoniae to invade and progression of disease in the host body. Besides the low mass on the cell surface, alpha-enolase possesses significant plasminogen binding among all exposed proteins.
methodsIn-silico based drug designing approach was implemented for evaluating potential inhibitors against alpha-enolase based on their binding affinities, energy score and pharmacokinetics. Lipinski's rule of five (LRo5) and Egan's (Brain Or IntestinaL EstimateD) BOILED-Egg methods were executed to predict the best ligand for biological systems.
resultsMolecular docking analysis revealed, Sodium (1,5-dihydroxy-2-oxopyrrolidin-3-yl)-hydroxy-dioxidophosphanium (SF-2312) as a promising inhibitor that fabricates finest attractive charges and conventional hydrogen bonds with S. pneumoniae alpha-enolase. Moreover, the pharmacokinetics of SF-2312 predict it as a therapeutic inhibitor for clinical trials. Like SF-2312, phosphono-acetohydroxamate (PhAH) also constructed adequate interactions at the active site of alpha-enolase, but it predicted less favourable than SF-2312 based on binding affinity.
conclusionBriefly, SF-2312 and PhAH ligands could inhibit the role of alpha-enolase to restrain plasminogen binding, invasion and progression of S. pneumoniae. As per our investigation and analysis, SF-2312 is the most potent naturally existing inhibitor of S. pneumoniae alpha-enolase in current time.
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