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Development of Highly Potent Inhibitors of the Ras-Targeting Human Acyl Protein Thioesterases Based on Substrate Similarity Design

Authors :
Christian Hedberg
Robin S. Bon
Steffen Renner
Frank J. Dekker
Claas Gerding-Reimers
Philippe I. H. Bastiaens
Stefan Wetzel
Herbert Waldmann
Nachiket Vartak
Marion Rusch
Medicinal Chemistry and Bioanalysis (MCB)
Biopharmaceuticals, Discovery, Design and Delivery (BDDD)
Source :
Angewandte Chemie, Angewandte Chemie-International Edition, 50(42), 9832-9837. WILEY-V C H VERLAG GMBH
Publication Year :
2011
Publisher :
Wiley, 2011.

Abstract

A matter of common sense: a common recognition motif consisting of a negatively charged group five to six bonds away (red) from the (thio)ester functionality (green) and a positively charged tail group ten to twelve bonds away (blue) was identified in two native acyl protein thioesterase 1 (APT1) substrates. This similarity led to the design of potent inhibitors of the Ras-depalmitoylating enzyme APT1.

Details

ISSN :
14337851
Volume :
50
Database :
OpenAIRE
Journal :
Angewandte Chemie International Edition
Accession number :
edsair.doi.dedup.....8918df67a9ab47becfd0f9300e6396c4
Full Text :
https://doi.org/10.1002/anie.201102965