Title

Structural basis for the in vitro known acyl-depsipeptide 2 (ADEP2) inhibition to Clp 2 protease from Mycobacterium tuberculosis

Authors

Natasha Khandekar1,2, Snehal Singh2, Ruchi Shukla2, Sridevi Tirumalaraju3, Srinivas Bandaru4, Tushar Banerjee1, Anuraj Nayarisseri2

Affiliation

1School of Life Science, Devi Ahilya University, Khandwa Road, Indore - 452 001, Madhya Pradesh, India; 2Bioinformatics Research Laboratory, Eminent Biosciences, Vijaynagar, Indore - 452010, India; 3Mahatma Gandhi National Institute of Research & Social Action, Hyderabad – 500029, India; 4Institute of Genetics and Hospital for Genetic Diseases, Osmania University, Hyderabad – 500 016, India.

Email

Anuraj Nayarisseri – E-mail: anuraj@eminentbio.com; *Corresponding author

Article Type

Hypothesis

Date

Received May 21, 2016; Accepted June 10, 2016; Published June 21, 2016

Inhibition of Mycobacterium tuberculosis Clp 2 protease has emerged as an attractive therapeutic option for treatment. Acyldepsipeptides (ADEPs) is known as an inhibitor for Clp 2 protease. Therefore, it is of interest to document its affinity, enzyme activity and ADME profiles. We report the predicted binding affinity of all known Clp 2 inhibitors like IDR-10001 and IDR-10011 against Clp2 protease using MolDock algorithm aided molecular docking. The predicted activity (using Molinspiration server) and ADMET properties (AdmetSAR server) were estimated for these compounds. This data suggest ADEP2 having improved binding features with Mtb Clp 2 having acceptable ADMET properties. This is in agreement with known in vitro data for ADEP2 inhibition with Mtb Clp 2 protease.

Keywords

Mycobacterium tuberculosis, Clp 2 protease, ADEPs, molecular docking, pharmacological profiling

Citation

Khandekar et al. Bioinformation 12(3): 92-97 (2016)

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.