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Inside Cover: A Highly Potent and Selective Caspase 1 Inhibitor that Utilizes a Key 3-Cyanopropanoic Acid Moiety (ChemMedChem 5/2010)

✍ Scribed by Matthew B. Boxer; Amy M. Quinn; Min Shen; Ajit Jadhav; William Leister; Anton Simeonov; Douglas S. Auld; Craig J. Thomas

Publisher: John Wiley and Sons
Year: 2010
Tongue: English
Weight: 528 KB
Volume: 5
Category: Article
ISSN: 1860-7179
DOI: 10.1002/cmdc.201090016

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✦ Synopsis

The inside cover picture shows the caspase 1 inhibitor NCGC00183434 modeled in the active site making key contacts between the cysteine of the enzyme and the nitrile group of the inhibitor, as well as key contacts between the aspartic acid mimetic and core arginine residues. NCGC00183434 was found to be a sub-nanomolar inhibitor with > 100-fold selectivity for caspase 1 over 10 other caspases. For more details, see the Full Paper by C. J. Thomas et al. on p. 730 ff.

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A Highly Potent and Selective Caspase 1

A Highly Potent and Selective Caspase 1 Inhibitor that Utilizes a Key 3-Cyanopropanoic Acid Moiety

✍ Matthew B. Boxer; Amy M. Quinn; Min Shen; Ajit Jadhav; William Leister; Anton Si 📂 Article 📅 2010 🏛 John Wiley and Sons 🌐 English ⚖ 493 KB

## Abstract __Herein, we examine the potential of a nitrile‐containing propionic acid moiety as an electrophile for covalent attack by the active‐site cysteine residue of caspase 1. The syntheses of several cyanopropanate‐containing small molecules based on the optimized peptidic scaffold of prodru