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Veale et al ChemRxiv 0610.pdf (1.72 MB)
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A New Native Mass Spectrometry Platform Identifies Inhibitors of the HSP90 – HOP Protein-Protein Interaction

preprint
submitted on 10.06.2020 and posted on 11.06.2020 by Clinton Veale, Mateos-Jimenez, Maria, Michaelone Vaaltyn, Ronel Müller, Matodzi Makhubu, Mahama Alhassan, Beatriz G. de la Torre, Fernando Albericio, C. Logan Mackay, Adrienne L. Edkins, David Clarke
This communication discusses for the first time, the use of mass spectrometry as a platform for screening for PPI inhibitors, without protein tethering or labeling. Furthermore, in the context of cancer drug discovery, this study demonstrates the ligandability and therefore the potential druggability of HOP, whose PPI with HSP90 has been routinely discussed as a difficult to drug target of substantial potential.

Funding

Underpinning UK Biomolecular Research with Next-Generation High Resolution Mass Spectrometry at the University of Edinburgh

Biotechnology and Biological Sciences Research Council

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University of KwaZulu-Natal Flagship Initiative

National Research Foundation of South Africa Grant Numbers 105829 116305 127224 98566

Royal Society Newton Fund Grant Number NI160018

Royal Society AAS FLAIR Fellowship

History

Email Address of Submitting Author

VealeC@ukzn.ac.za

Institution

University of KwaZulu-Natal

Country

South Africa

ORCID For Submitting Author

0000-0002-4043-7106

Declaration of Conflict of Interest

No conflict of interest to declare

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