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 predic...

Descripción completa

Detalles Bibliográficos
Autores principales: Khandekar, Natasha, Singh, Snehal, Shukla, Ruchi, Tirumalaraju, Sridevi, Bandaru, Srinivas, Banerjee, Tushar, Nayarisseri, Anuraj
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Biomedical Informatics 2016
Materias:
Hypothesis
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5267950/
https://www.ncbi.nlm.nih.gov/pubmed/28149041
http://dx.doi.org/10.6026/97320630012092
_version_ 1782500725271560192
author Khandekar, Natasha
Singh, Snehal
Shukla, Ruchi
Tirumalaraju, Sridevi
Bandaru, Srinivas
Banerjee, Tushar
Nayarisseri, Anuraj
author_facet Khandekar, Natasha
Singh, Snehal
Shukla, Ruchi
Tirumalaraju, Sridevi
Bandaru, Srinivas
Banerjee, Tushar
Nayarisseri, Anuraj
author_sort Khandekar, Natasha
collection PubMed
description 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.
format Online
Article
Text
id pubmed-5267950
institution National Center for Biotechnology Information
language English
publishDate 2016
publisher Biomedical Informatics
record_format MEDLINE/PubMed
spelling pubmed-52679502017-02-01 Structural basis for the in vitro known acyl-depsipeptide 2 (ADEP2) inhibition to Clp 2 protease from Mycobacterium tuberculosis Khandekar, Natasha Singh, Snehal Shukla, Ruchi Tirumalaraju, Sridevi Bandaru, Srinivas Banerjee, Tushar Nayarisseri, Anuraj Bioinformation Hypothesis 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. Biomedical Informatics 2016-06-21 /pmc/articles/PMC5267950/ /pubmed/28149041 http://dx.doi.org/10.6026/97320630012092 Text en © 2016 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.
spellingShingle Hypothesis
Khandekar, Natasha
Singh, Snehal
Shukla, Ruchi
Tirumalaraju, Sridevi
Bandaru, Srinivas
Banerjee, Tushar
Nayarisseri, Anuraj
Structural basis for the in vitro known acyl-depsipeptide 2 (ADEP2) inhibition to Clp 2 protease from Mycobacterium tuberculosis
title Structural basis for the in vitro known acyl-depsipeptide 2 (ADEP2) inhibition to Clp 2 protease from Mycobacterium tuberculosis
title_full Structural basis for the in vitro known acyl-depsipeptide 2 (ADEP2) inhibition to Clp 2 protease from Mycobacterium tuberculosis
title_fullStr Structural basis for the in vitro known acyl-depsipeptide 2 (ADEP2) inhibition to Clp 2 protease from Mycobacterium tuberculosis
title_full_unstemmed Structural basis for the in vitro known acyl-depsipeptide 2 (ADEP2) inhibition to Clp 2 protease from Mycobacterium tuberculosis
title_short Structural basis for the in vitro known acyl-depsipeptide 2 (ADEP2) inhibition to Clp 2 protease from Mycobacterium tuberculosis
title_sort structural basis for the in vitro known acyl-depsipeptide 2 (adep2) inhibition to clp 2 protease from mycobacterium tuberculosis
topic Hypothesis
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5267950/
https://www.ncbi.nlm.nih.gov/pubmed/28149041
http://dx.doi.org/10.6026/97320630012092
work_keys_str_mv AT khandekarnatasha structuralbasisfortheinvitroknownacyldepsipeptide2adep2inhibitiontoclp2proteasefrommycobacteriumtuberculosis
AT singhsnehal structuralbasisfortheinvitroknownacyldepsipeptide2adep2inhibitiontoclp2proteasefrommycobacteriumtuberculosis
AT shuklaruchi structuralbasisfortheinvitroknownacyldepsipeptide2adep2inhibitiontoclp2proteasefrommycobacteriumtuberculosis
AT tirumalarajusridevi structuralbasisfortheinvitroknownacyldepsipeptide2adep2inhibitiontoclp2proteasefrommycobacteriumtuberculosis
AT bandarusrinivas structuralbasisfortheinvitroknownacyldepsipeptide2adep2inhibitiontoclp2proteasefrommycobacteriumtuberculosis
AT banerjeetushar structuralbasisfortheinvitroknownacyldepsipeptide2adep2inhibitiontoclp2proteasefrommycobacteriumtuberculosis
AT nayarisserianuraj structuralbasisfortheinvitroknownacyldepsipeptide2adep2inhibitiontoclp2proteasefrommycobacteriumtuberculosis

Ejemplares similares