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Structure-Based Virtual Screening of Essential Mycobacterium Tuberculosis Enzymes AspS and KatG for potential inhibitors


Andrew P. Collins1, * & Waleed Abdelfattah2



1University of Central Florida College of Medicine, Orlando, Florida; 2University of Washington, Seattle, WA;



Andrew P. Collins Email ID - Andrewcollins@knights.ucf.edu


Article Type

Research Article



Received July 21, 2020; Revised December 31, 2020; Accepted January 26, 2020, Published January 31, 2021



Mycobacterium tuberculosis (TB) is a leading global cause of disease-related death. Recent works have studied metabolic pathways of the mycobacterium, highlighting essential enzymes to target via competitive inhibition through computational molecular modeling to suppress the organismís life cycle. We used the Protein Databank (PDB), the UniProt Knowledgebase and the iDock server in this study. In vitro toxicity screening and pharmacokinetic properties were assessed to determine potential ligand safety and drug properties. Our results have revealed five and nine potential ligands for the enzymes AspS and KatG respectively. The KatG active site has displayed binding affinities of -13.443 to -12.895 kcal/mol, while AspS ligands range from -6.580 to -6.490kcal/mol. The intermolecular forces responsible for the differing binding affinities of each enzyme are primarily Coulombic interactions for AspS, versus Coulombic and extensive hydrogen bonding interactions in KatG.





Collins & Abdelfattah, Bioinformation 17(1): 101-108 (2021)

Edited by

P Kangueane






Biomedical Informatics



This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.