Jump to main content
Jump to site search

Issue 67, 2017
Previous Article Next Article

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

Author affiliations

Abstract

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.

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

Back to tab navigation

Supplementary files

Publication details

The article was received on 12 Jul 2017, accepted on 02 Aug 2017 and first published on 02 Aug 2017


Article type: Communication
DOI: 10.1039/C7CC05379G
Citation: Chem. Commun., 2017,53, 9372-9375
  • Open access: Creative Commons BY license
  •   Request permissions

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

    D. J. Cole, M. Janecek, J. E. Stokes, M. Rossmann, J. C. Faver, G. J. McKenzie, A. R. Venkitaraman, M. Hyvönen, D. R. Spring, D. J. Huggins and W. L. Jorgensen, Chem. Commun., 2017, 53, 9372
    DOI: 10.1039/C7CC05379G

    This article is licensed under a Creative Commons Attribution 3.0 Unported Licence. Material from this article can be used in other publications provided that the correct acknowledgement is given with the reproduced material.

    Reproduced material should be attributed as follows:

    • For reproduction of material from NJC:
      [Original citation] - Published by The Royal Society of Chemistry (RSC) on behalf of the Centre National de la Recherche Scientifique (CNRS) and the RSC.
    • For reproduction of material from PCCP:
      [Original citation] - Published by the PCCP Owner Societies.
    • For reproduction of material from PPS:
      [Original citation] - Published by The Royal Society of Chemistry (RSC) on behalf of the European Society for Photobiology, the European Photochemistry Association, and RSC.
    • For reproduction of material from all other RSC journals:
      [Original citation] - Published by The Royal Society of Chemistry.

    Information about reproducing material from RSC articles with different licences is available on our Permission Requests page.

Search articles by author

Spotlight

Advertisements