Abstract

The HECT E3 ubiquitin ligases 1 (WWP1) and 2 (WWP2) are responsible for the ubiquitin-mediated degradation of key tumour suppressor proteins and are dysregulated in various cancers and diseases. Here we expand their limited inhibitor space by identification of NSC-217913 displaying a WWP1 IC50 of 158.3 µM (95% CI = 128.7, 195.1 µM). A structure-activity relationship by synthesis approach aided by molecular docking led to compound 11 which displayed increased potency with an IC50 of 32.7 µM (95% CI = 24.6, 44.3 µM) for WWP1 and 269.2 µM (95% CI = 209.4, 347.9 µM) for WWP2. Molecular docking yielded active site-bound poses suggesting that the heterocyclic imidazo[4,5-b]pyrazine scaffold undertakes a π-stacking interaction with the phenolic group of tyrosine, and the ethyl ester enables strong ion-dipole interactions. Given the therapeutic potential of WWP1 and WWP2, we propose that compound 11 may provide a basis for future lead compound development.

Details

Title
Expanding the inhibitor space of the WWP1 and WWP2 HECT E3 ligases
Author
Dudey, Ashley P 1 ; Rigby, Jake M 2 ; Hughes, Gregory R 1 ; Stephenson, G Richard 2 ; Storr, Thomas E 2 ; Chantry, Andrew 1 ; Hemmings, Andrew M 3 

 School of Biological Sciences, University of East Anglia, Norwich, UK 
 School of Chemistry, Pharmacy & Pharmacology, University of East Anglia, Norwich, UK 
 School of Biological Sciences, University of East Anglia, Norwich, UK; School of Chemistry, Pharmacy & Pharmacology, University of East Anglia, Norwich, UK; International Research Center for Food and Health, College of Food Science and Technology, Shanghai Ocean University, Shanghai, China 
Publication year
2024
Publication date
Dec 2024
Publisher
Taylor & Francis Ltd.
ISSN
14756366
e-ISSN
14756374
Source type
Scholarly Journal
Language of publication
English
ProQuest document ID
3149477055
Copyright
© 2024 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group. This work is licensed under the Creative Commons Attribution License http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.