Molecular docking simulation analysis of the interaction of dietary flavonols with heat shock protein 90

Hsp90 is a major protein involved in the stabilization of various proteins in cancer cells. The present investigation focused on the molecular docking simulation studies of flavanols as inhibitors of Hsp90 at the high affinity adenosine triphosphate (ATP) binding site and analyzed absorption, distri...

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Detalles Bibliográficos
Autores principales: Singh, Salam Pradeep, Deb, Chitta Ranjan, Ahmed, Sharif Udin, Saratchandra, Yenisetti, Konwar, Bolin Kumar
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Editorial Department of Journal of Biomedical Research 2016
Materias:
Original Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4726836/
http://dx.doi.org/10.7555/JBR.30.20130158
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author Singh, Salam Pradeep
Deb, Chitta Ranjan
Ahmed, Sharif Udin
Saratchandra, Yenisetti
Konwar, Bolin Kumar
author_facet Singh, Salam Pradeep
Deb, Chitta Ranjan
Ahmed, Sharif Udin
Saratchandra, Yenisetti
Konwar, Bolin Kumar
author_sort Singh, Salam Pradeep
collection PubMed
description Hsp90 is a major protein involved in the stabilization of various proteins in cancer cells. The present investigation focused on the molecular docking simulation studies of flavanols as inhibitors of Hsp90 at the high affinity adenosine triphosphate (ATP) binding site and analyzed absorption, distribution, metabolism, excretion and toxicity (ADME-toxicity). The molecular docking analysis revealed that the flavanols showed competitive inhibition with ATP molecule at the active site and enhanced pharmacological parameters.
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spelling pubmed-47268362016-01-31 Molecular docking simulation analysis of the interaction of dietary flavonols with heat shock protein 90 Singh, Salam Pradeep Deb, Chitta Ranjan Ahmed, Sharif Udin Saratchandra, Yenisetti Konwar, Bolin Kumar J Biomed Res Original Article Hsp90 is a major protein involved in the stabilization of various proteins in cancer cells. The present investigation focused on the molecular docking simulation studies of flavanols as inhibitors of Hsp90 at the high affinity adenosine triphosphate (ATP) binding site and analyzed absorption, distribution, metabolism, excretion and toxicity (ADME-toxicity). The molecular docking analysis revealed that the flavanols showed competitive inhibition with ATP molecule at the active site and enhanced pharmacological parameters. Editorial Department of Journal of Biomedical Research 2016-01 2015-06-08 /pmc/articles/PMC4726836/ http://dx.doi.org/10.7555/JBR.30.20130158 Text en 2016 the Journal of Biomedical Research. All rights reserved.
spellingShingle Original Article
Singh, Salam Pradeep
Deb, Chitta Ranjan
Ahmed, Sharif Udin
Saratchandra, Yenisetti
Konwar, Bolin Kumar
Molecular docking simulation analysis of the interaction of dietary flavonols with heat shock protein 90
title Molecular docking simulation analysis of the interaction of dietary flavonols with heat shock protein 90
title_full Molecular docking simulation analysis of the interaction of dietary flavonols with heat shock protein 90
title_fullStr Molecular docking simulation analysis of the interaction of dietary flavonols with heat shock protein 90
title_full_unstemmed Molecular docking simulation analysis of the interaction of dietary flavonols with heat shock protein 90
title_short Molecular docking simulation analysis of the interaction of dietary flavonols with heat shock protein 90
title_sort molecular docking simulation analysis of the interaction of dietary flavonols with heat shock protein 90
topic Original Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4726836/
http://dx.doi.org/10.7555/JBR.30.20130158
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