Screening and Identification of Natural Compounds as Potential Inhibitors of Glutamate Racemase, an Emerging Drug Target of Food Pathogen E. coli O157:H7: An In-silico Approach to Combat Increasing Drug Resistance
Kumar R. Gupta S. Adhana S. Khanna A. Sahoo S. Faiza M. Baweja R. Pandey A. Mittal A. Chaudhry U.
2025Bentham Science Publishers
Infectious Disorders - Drug Targets
2025#25Issue 2
Background: Shiga Toxin-Producing Escherichia coli (E. coli) O157:H7, capable of causing serious food-borne illnesses, is extensively studied and is known to be transmitted through animal reservoirs or person-to-person contact, leading to severe disease outbreaks. The emergence of antibiotic resistance in these strains, coupled with increased adverse effects of existing therapeutics, underscores the urgent need for alternative therapeutic strategies. Objective: This study aims to evaluate Glutamate Racemase (MurI protein) of the food-pathogenic E. coli O157:H7 (EC MurI) as a novel drug target. Furthermore, the study seeks to identify new compounds with potential inhibitory effects against this protein. Methods: Using computational tools, the study identified inhibitor binding sites on EC MurI and identified relevant inhibitors capable of binding to these sites. Molecular docking techniques were employed to assess potential hits, and selected compounds were further analyzed for their structural activity and binding affinity to the protein. Results: The results of the study revealed that Frigocyclinone and Deslanoside, exhibited the best binding affinity with EC-MurI. Subsequent molecular dynamic (MD) simulations of the selected complexes indicated that both compounds were stable. This suggests that Frigocyclinone and Deslanoside have the potential to serve as potent inhibitors of EC-MurI. Conclusion: In summary, this study highlights the urgent need for alternative therapies against food-pathogenic E. coli, focusing on E. coli O157:H7. Evaluation of Glutamate Racemase as a drug target identified Frigocyclinone and Deslanoside as promising inhibitors. MD simulations indicated their stability, suggesting their potential as lead molecules for further research and treatment development.
antibiotic resistance , docking , EC-MurI , glutamate racemase , inhibitors , peptidoglycan , Shiga toxin-producing E.coli
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Department of Biomedical Science, Bhaskaracharya College of Applied Sciences, University of Delhi, Sector-2, Phase-I, Dwarka, New Delhi, 110075, India
Membrane Protein Biology Group, ICGEB, Aruna Asaf Ali Marg, New Delhi, 110067, India
Department of Biology, Nazarbayev University, Qabanbay Batyr Avenue, Nur-Sultan, Kazakhstan
Department of Biochemistry, Shivaji College, University of Delhi, Mahatma Gandhi Rd, Shivaji Enclave, Raja Garden, Delhi, 110027, India
Department of Biomedical Science, Acharya Narendra Dev College, University of Delhi, Govindpuri, KalkaJi, New Delhi, 110019, India
Department of Electronics, Bhaskaracharya College of Applied Sciences, University of Delhi, Sector-2, Phase-I, Dwarka, New Delhi, 110075, India
Department of Biomedical Science
Membrane Protein Biology Group
Department of Biology
Department of Biochemistry
Department of Biomedical Science
Department of Electronics
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