A potential lead compound to overcome dapsone resistance in M. leprae folP1 was identified by a virtual screening strategy.

Ramanathan K

Department of Biotechnology

School of Bio Sciences and Technology

Vellore Campus

Nawaz Khan F

Department of Chemistry

School of Advanced Sciences

Shanthi V

Nisha J

Dhanasekaran D

Vellore Institute of Technology (VIT) is a private university located in&nbsp;Tamil Nadu, India. Founded in 1984, as Vellore Engineering College, the institution offers 20 undergraduate, 34 postgraduate, four integrated and four research programs. It has campuses in Vellore, Amravati, Bhopal and Chennai.

VIT is one of the top ranked private universities in India according to NIRF, THE and QS Rankings.&nbsp;Govt. of India has recognized&nbsp;VIT, Vellore as an&nbsp;Institution of Eminence. This has allowed VIT to take independent quality initiatives and move up in world ranking.

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VIT University

Molecular BioSystems

Mycobacterium leprae, the etiologic agent of leprosy, is non-cultivable in vitro. Consequently, the assessment of antibiotic activity against M. leprae hinge mainly upon the time consuming mouse footpad system. As M. leprae develops resistance against most of the drugs, the evolution of new long acting antimycobacterial compounds stand in need for leprosy control. The rpoB of M. leprae is the target of antimycobacterial drug, rifampicin. Recently, cases were reported that rpoB mutation (S425L) became resistant to rifampicin and the mechanism of resistance is still not well understood. The present study is aimed at studying the molecular and structural mechanism of the rifampicin binding to both native and mutant rpoB through computational approaches. From molecular docking, we demonstrated the stable binding of rifampicin through two hydrogen bonding with His420 residue of native than with mutant rpoB where one hydrogen bonding was found with Ser406. The difference in binding energies observed in the docking study evidently signifies that rifampicin is less effective in the treatment of patients with S425L variant. Moreover, the molecular dynamics studies also highlight the stable binding of rifampicin with native than mutant (S425L) rpoB. J. Cell. Biochem. 116: 1278-1285, 2015. © 2015 Wiley Periodicals, Inc. © 2015 Wiley Periodicals, Inc.

Journal of Cellular Biochemistry

Computational Simulation Techniques to Understand Rifampicin Resistance Mutation (S425L) ofrpoBinM. leprae

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PLoS ONE

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Journal of the American Chemical Society

Recognition of Imipenem and Meropenem by the RND-Transporter MexB Studied by Computer Simulations

Discovery of a potential lead compound for treating leprosy with dapsone resistance mutation in M. leprae folP1

Journal	Data powered by TypesetMolecular BioSystems
Publisher	Data powered by TypesetRoyal Society of Chemistry (RSC)
ISSN	1742-206X
Open Access	0