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Discovery of high affinity inhibitors of Leishmania donovani N-myristoyltransferase

DOI: 10.1039/C5MD00241A DOI Help

Authors: Mark D. Rackham (Imperial College London) , Zhiyong Yu (Imperial College London) , James A. Brannigan (University of York) , William P. Heal (Imperial College London) , Daniel Paape (University of York) , K. Victoria Barker (Imperial College London) , Anthony J. Wilkinson (University of York) , Deborah F. Smith (University of York) , Robin J. Leatherbarrow (Imperial College London) , Edward W. Tate (Imperial College London)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Medchemcomm , VOL 6 (10) , PAGES 1761 - 1766

State: Published (Approved)
Published: August 2015

Abstract: N-Myristoyltransferase (NMT) is a potential drug target in Leishmania parasites. Scaffold-hopping from published inhibitors yielded the serendipitous discovery of a chemotype selective for Leishmania donovani NMT; development led to high affinity inhibitors with excellent ligand efficiency. The binding mode was characterised by crystallography and provides a structural rationale for selectivity.

Subject Areas: Chemistry


Instruments: I04-1-Macromolecular Crystallography (fixed wavelength)