Molecular docking and pharmacophore studies of heterocyclic compounds as Heat shock protein 90 (Hsp90) Inhibitors

Heat Shock Protein 90 was a key molecular chaperone involved in the proteome stability maintenance and its interference in many signaling networks associated with cancer progression, makes it of an important target for cancer therapeutics. The present study aimed to identify potential lead molecule...

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Autores principales: Baby, Suby T, Sharma, Shailendra, Enaganti, Sreenivas, Cherian, P. Roby
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Biomedical Informatics 2016
Materias:
Hypothesis
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5289218/
https://www.ncbi.nlm.nih.gov/pubmed/28232775
http://dx.doi.org/10.6026/97320630012149
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author Baby, Suby T
Sharma, Shailendra
Enaganti, Sreenivas
Cherian, P. Roby
author_facet Baby, Suby T
Sharma, Shailendra
Enaganti, Sreenivas
Cherian, P. Roby
author_sort Baby, Suby T
collection PubMed
description Heat Shock Protein 90 was a key molecular chaperone involved in the proteome stability maintenance and its interference in many signaling networks associated with cancer progression, makes it of an important target for cancer therapeutics. The present study aimed to identify potential lead molecule among the selected heterocyclic compounds against Human Hsp90 (PDB: 1YET) through docking using GOLD 3.1 and pharmacophore studies using Discovery studio 2.1. On the basis of the GOLD Fitness scores, the compounds Q1G and T21 showed better binding affinity. Further the analyzed structure pharmacophore results are in consistence with the docking results indicating that both these compounds show antagonistic activity towards HSP90 respectively.
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spelling pubmed-52892182017-02-23 Molecular docking and pharmacophore studies of heterocyclic compounds as Heat shock protein 90 (Hsp90) Inhibitors Baby, Suby T Sharma, Shailendra Enaganti, Sreenivas Cherian, P. Roby Bioinformation Hypothesis Heat Shock Protein 90 was a key molecular chaperone involved in the proteome stability maintenance and its interference in many signaling networks associated with cancer progression, makes it of an important target for cancer therapeutics. The present study aimed to identify potential lead molecule among the selected heterocyclic compounds against Human Hsp90 (PDB: 1YET) through docking using GOLD 3.1 and pharmacophore studies using Discovery studio 2.1. On the basis of the GOLD Fitness scores, the compounds Q1G and T21 showed better binding affinity. Further the analyzed structure pharmacophore results are in consistence with the docking results indicating that both these compounds show antagonistic activity towards HSP90 respectively. Biomedical Informatics 2016-06-15 /pmc/articles/PMC5289218/ /pubmed/28232775 http://dx.doi.org/10.6026/97320630012149 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
Baby, Suby T
Sharma, Shailendra
Enaganti, Sreenivas
Cherian, P. Roby
Molecular docking and pharmacophore studies of heterocyclic compounds as Heat shock protein 90 (Hsp90) Inhibitors
title Molecular docking and pharmacophore studies of heterocyclic compounds as Heat shock protein 90 (Hsp90) Inhibitors
title_full Molecular docking and pharmacophore studies of heterocyclic compounds as Heat shock protein 90 (Hsp90) Inhibitors
title_fullStr Molecular docking and pharmacophore studies of heterocyclic compounds as Heat shock protein 90 (Hsp90) Inhibitors
title_full_unstemmed Molecular docking and pharmacophore studies of heterocyclic compounds as Heat shock protein 90 (Hsp90) Inhibitors
title_short Molecular docking and pharmacophore studies of heterocyclic compounds as Heat shock protein 90 (Hsp90) Inhibitors
title_sort molecular docking and pharmacophore studies of heterocyclic compounds as heat shock protein 90 (hsp90) inhibitors
topic Hypothesis
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5289218/
https://www.ncbi.nlm.nih.gov/pubmed/28232775
http://dx.doi.org/10.6026/97320630012149
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