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

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Title	`Structure-Based Virtual Screening of Essential Mycobacterium Tuberculosis Enzymes AspS and KatG for potential inhibitors`
Authors	`Andrew P. Collins^1, & Waleed Abdelfattah²`*
Affiliation	`¹University of Central Florida College of Medicine, Orlando, Florida; ²University of Washington, Seattle, WA;`
Email	`Andrew P. Collins Email ID - Andrewcollins@knights.ucf.edu`
Article Type	`Research Article`
Date	`Received July 21, 2020; Revised December 31, 2020; Accepted January 26, 2020, Published January 31, 2021`
Abstract	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 organism’s 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.
Keywords
Citation	`Collins & Abdelfattah,` `Bioinformation 17(1): 101-108 (2021)`
Edited by	P Kangueane
ISSN	0973-2063
Publisher	Biomedical Informatics
License	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.