ACS Medicinal Chemistry Letters · 2012 · 44 citations · 21 references
PharmacyMedicinal ChemistryPharmacologyBioisosterismDrug DiscoveryLead OptimizationHit-to-lead OptimizationNeuroprotectionPotency OptimizationSolubility OptimizationBrain ExposureCompound Potency OptimizationDrug Candidate OptimizationMolecular Property Modulation By Bioisosteric SubstitutionParkinson's Disease PharmacotherapyParkinson’s Disease PharmacotherapyRodent NeuropharmacologySolubility
The modulation of LRRK2 kinase activity by a selective small molecule inhibitor has been proposed as a potentially viable treatment for Parkinson's disease. By using aminopyrazoles as aniline bioisosteres, we discovered a novel series of LRRK2 inhibitors. Herein, we describe our optimization effort that resulted in the identification of a highly potent, brain-penetrant aminopyrazole LRRK2 inhibitor (18) that addressed the liabilities (e.g., poor solubility and metabolic soft spots) of our previously disclosed anilino-aminopyrimidine inhibitors. In in vivo rodent PKPD studies, 18 demonstrated good brain exposure and engendered significant reduction in brain pLRRK2 levels post-ip administration. The strategies of bioisosteric substitution of aminopyrazoles for anilines and attenuation of CYP1A2 inhibition described herein have potential applications to other drug discovery programs.
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Mutations in LRRK2 Cause Autosomal-Dominant Parkinsonism with Pleomorphic Pathology
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Cloning of the Gene Containing Mutations that Cause PARK8-Linked Parkinson's Disease
Coro Paisán-Ruı́z, Shushant Jain, E. Whitney Evans et al. · Neuron · 2004 · 2.4K citations · Full text
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