Journal of Medicinal Chemistry · 2019 · 91 citations · 14 references
PharmacyMedicinal ChemistryPharmacologyDrug DiscoveryLead OptimizationStructure-activity RelationshipsEnzyme InhibitionLead Compound DesignLigand BindingLigand-based DesignStructure-activity Relationship AnalysisBenzoic Acid DerivativesCancer Cell Line ModelsChemical Scaffold OptimizationMedicinal Chemistry ApplicationsPharmacological PotencySalt Bridge FormationX-ray Diffraction AnalysisX-ray Structure Determination
We report the discovery of a potent and isozyme-selective MTHFD2 inhibitor, DS18561882 (2). Through investigation of the substituents on our tricyclic coumarin scaffold (1,2,3,4-tetrahydrochromeno[3,4-c]pyridin-5-one), MTHFD2 inhibitory activity was shown to be elevated by incorporating an amine moiety at the 8-position and a methyl group at the 7-position of the initial lead 1. X-ray structure analysis revealed that a key interaction for enhanced potency was salt bridge formation between the amine moiety and the diphosphate linker of an NAD+ cofactor. Furthermore, ortho-substituted sulfonamide in place of benzoic acid of 1 significantly improved cell permeability and cell-based growth inhibition against a human breast cancer cell line. The thus-optimized DS18561882 showed the strongest cell-based activity (GI50 = 140 nM) in the class, a good oral pharmacokinetic profile, and thereby tumor growth inhibition in a mouse xenograft model upon oral administration.
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Increased MTHFD2 expression is associated with poor prognosis in breast cancer
Yang Liu, Chuan He, Xiaoguang He et al. · Tumor Biology · 2014 · 111 citations
Medicine, Cancer Biology, Oncology +15