Computationally-guided optimization of small-molecule inhibitors of the Aurora A kinase–TPX2 protein–protein interaction

Free energy perturbation theory, in combination with enhanced sampling of protein–ligand binding modes, is evaluated in the context of fragment-based drug design, and used to design two new small-molecule inhibitors of the Aurora A kinase–TPX2 protein–protein interaction.

Detalles Bibliográficos
Autores principales: Cole, Daniel J., Janecek, Matej, Stokes, Jamie E., Rossmann, Maxim, Faver, John C., McKenzie, Grahame J., Venkitaraman, Ashok R., Hyvönen, Marko, Spring, David R., Huggins, David J., Jorgensen, William L.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Royal Society of Chemistry 2017
Materias:
Chemistry
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5591577/
https://www.ncbi.nlm.nih.gov/pubmed/28787041
http://dx.doi.org/10.1039/c7cc05379g
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author Cole, Daniel J.
Janecek, Matej
Stokes, Jamie E.
Rossmann, Maxim
Faver, John C.
McKenzie, Grahame J.
Venkitaraman, Ashok R.
Hyvönen, Marko
Spring, David R.
Huggins, David J.
Jorgensen, William L.
author_facet Cole, Daniel J.
Janecek, Matej
Stokes, Jamie E.
Rossmann, Maxim
Faver, John C.
McKenzie, Grahame J.
Venkitaraman, Ashok R.
Hyvönen, Marko
Spring, David R.
Huggins, David J.
Jorgensen, William L.
author_sort Cole, Daniel J.
collection PubMed
description Free energy perturbation theory, in combination with enhanced sampling of protein–ligand binding modes, is evaluated in the context of fragment-based drug design, and used to design two new small-molecule inhibitors of the Aurora A kinase–TPX2 protein–protein interaction.
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spelling pubmed-55915772018-05-18 Computationally-guided optimization of small-molecule inhibitors of the Aurora A kinase–TPX2 protein–protein interaction Cole, Daniel J. Janecek, Matej Stokes, Jamie E. Rossmann, Maxim Faver, John C. McKenzie, Grahame J. Venkitaraman, Ashok R. Hyvönen, Marko Spring, David R. Huggins, David J. Jorgensen, William L. Chem Commun (Camb) Chemistry Free energy perturbation theory, in combination with enhanced sampling of protein–ligand binding modes, is evaluated in the context of fragment-based drug design, and used to design two new small-molecule inhibitors of the Aurora A kinase–TPX2 protein–protein interaction. Royal Society of Chemistry 2017-08-28 2017-08-02 /pmc/articles/PMC5591577/ /pubmed/28787041 http://dx.doi.org/10.1039/c7cc05379g Text en This journal is © The Royal Society of Chemistry 2017 http://creativecommons.org/licenses/by/3.0/ This article is freely available. This article is licensed under a Creative Commons Attribution 3.0 Unported Licence (CC BY 3.0)
spellingShingle Chemistry
Cole, Daniel J.
Janecek, Matej
Stokes, Jamie E.
Rossmann, Maxim
Faver, John C.
McKenzie, Grahame J.
Venkitaraman, Ashok R.
Hyvönen, Marko
Spring, David R.
Huggins, David J.
Jorgensen, William L.
Computationally-guided optimization of small-molecule inhibitors of the Aurora A kinase–TPX2 protein–protein interaction
title Computationally-guided optimization of small-molecule inhibitors of the Aurora A kinase–TPX2 protein–protein interaction
title_full Computationally-guided optimization of small-molecule inhibitors of the Aurora A kinase–TPX2 protein–protein interaction
title_fullStr Computationally-guided optimization of small-molecule inhibitors of the Aurora A kinase–TPX2 protein–protein interaction
title_full_unstemmed Computationally-guided optimization of small-molecule inhibitors of the Aurora A kinase–TPX2 protein–protein interaction
title_short Computationally-guided optimization of small-molecule inhibitors of the Aurora A kinase–TPX2 protein–protein interaction
title_sort computationally-guided optimization of small-molecule inhibitors of the aurora a kinase–tpx2 protein–protein interaction
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5591577/
https://www.ncbi.nlm.nih.gov/pubmed/28787041
http://dx.doi.org/10.1039/c7cc05379g
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