Structural basis for the in vitro known acyl-depsipeptide 2 (ADEP2) inhibition to Clp 2 protease from Mycobacterium tuberculosis.
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.
School of Life Science, Devi Ahilya University, Khandwa Road, Indore - 452 001, Madhya Pradesh, India.; Bioinformatics Research Laboratory, Eminent Biosciences, Vijaynagar, Indore - 452010, India.
Natasha
N
Khandekar
Bioinformatics Research Laboratory, Eminent Biosciences, Vijaynagar, Indore - 452010, India.
Snehal
S
Singh
Bioinformatics Research Laboratory, Eminent Biosciences, Vijaynagar, Indore - 452010, India.
Ruchi
R
Shukla
Mahatma Gandhi National Institute of Research & Social Action,Hyderabad - 500029, India.
Sridevi
S
Tirumalaraju
Institute of Genetics and Hospital for Genetic Diseases, Osmania University, Hyderabad - 500 016, India.
Srinivas
S
Bandaru
School of Life Science, Devi Ahilya University, Khandwa Road, Indore - 452 001, Madhya Pradesh, India.
Tushar
T
Banerjee
Bioinformatics Research Laboratory, Eminent Biosciences, Vijaynagar, Indore - 452010, India.
Anuraj
A
Nayarisseri
ADEPs; Clp 2 protease; Mycobacterium tuberculosis; molecular docking; pharmacological profiling