ACS Medicinal Chemistry Letters · 2018 · 27 citations · 16 references
PharmacyMedicinal ChemistryPharmacologyDrug DesignDrug DiscoveryMolecular PharmacologyCovalent Drug DesignCovalent Inhibitor DesignEnzyme InhibitionLigand BindingPotency OptimizationTyrosine Kinase InhibitorsBruton Tyrosine KinaseBruton's Tyrosine Kinase InhibitorsBtk InhibitorsCovalent InhibitorsEgfr InhibitionReversible Covalent InhibitionReversible Covalent InhibitorsTyrosine Kinase Inhibition
Potent covalent inhibitors of Bruton's tyrosine kinase (BTK) based on an aminopyrazole carboxamide scaffold have been identified. Compared to acrylamide-based covalent reactive groups leading to irreversible protein adducts, cyanamide-based reversible-covalent inhibitors provided the highest combined BTK potency and EGFR selectivity. The cyanamide covalent mechanism with BTK was confirmed through enzyme kinetic, NMR, MS, and X-ray crystallographic studies. The lead cyanamide-based inhibitors demonstrated excellent kinome selectivity and rat pharmacokinetic properties.
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Lee Honigberg, Ashley M. Smith, Mint Sirisawad et al. · Proceedings of the National Academy of Sciences · 2010 · 1.5K citations · Full text
Discovery of Selective Irreversible Inhibitors for Bruton’s Tyrosine Kinase
Zhengying Pan, Heleen Scheerens, Shyr‐Jiann Li et al. · ChemMedChem · 2006 · 675 citations