A new publication in J Med chem for Pr Thierry Besson from the Heterocycle’s team managed by Dr Vincent Levacher, dealing with powerful inhibitors of DYRK’s family kinases (EHT 5372 and EHT 1610 have been designed in collaboration with DIAXONHIT). The published crystal structures of the complex revealed a non-canonical binding mode of both compounds in DYRK2 explaining the striking selectivity and potency of these inhibitors. It was noted that these compounds are currently the most active inhibitors for the DYRK family.
“An Unusual Binding Model of the Methyl 9-Anilinothiazolo[5,4-f]quinazoline-2-carbimidates (EHT 1610 and EHT 5372) Confers HighSelectivity for Dual-specificity Tyrosine Phosphorylation-Regulated Kinases.” Apirat Chaikuad, Julien Diharce, Martin Schröder, Alicia Foucourt, Bertrand Leblond, Anne-Sophie Casagrande, Laurent Desire, Pascal Bonnet, Stefan Knapp, and Thierry Besson
J. Med. Chem. 2016, Just Accepted Manuscript • DOI: 10.1021/acs.jmedchem.6b01083