Front Cover: Computationally Empowered Workflow Identifies Novel Covalent Allosteric Binders for KRASG12C (ChemMedChem 10/2020)

The Front Cover illustrates a novel inhibitor covalently bound to KRASG12C with an unprecedented mode of binding (image made with LigandScout). This discovery is the outcome of a computationally driven workflow based on the enumeration of novel chemical matter and stepwise prioritization. The most p...

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Published inChemMedChem Vol. 15; no. 10; p. 808
Main Authors Mortier, Jérémie, Friberg, Anders, Badock, Volker, Moosmayer, Dieter, Schroeder, Jens, Steigemann, Patrick, Siegel, Franziska, Gradl, Stefan, Bauser, Marcus, Hillig, Roman C., Briem, Hans, Eis, Knut, Bader, Benjamin, Nguyen, Duy, Christ, Clara D.
Format Journal Article
LanguageEnglish
Published 19.05.2020
Subjects
free-energy perturbation (FEP)
KRAS
medicinal chemistry
molecular dynamics
virtual library design
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Summary:The Front Cover illustrates a novel inhibitor covalently bound to KRASG12C with an unprecedented mode of binding (image made with LigandScout). This discovery is the outcome of a computationally driven workflow based on the enumeration of novel chemical matter and stepwise prioritization. The most promising compounds were synthesized, biochemically tested, and co‐crystallized with KRASG12C. More information can be found in the Communication by Jérémie Mortier, Duy Nguyen, Clara D.Christ et al.
ISSN:1860-7179
1860-7187
DOI:10.1002/cmdc.202000297