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1.
Bioorg Med Chem Lett ; 19(23): 6529-33, 2009 Dec 01.
Article in English | MEDLINE | ID: mdl-19857967

ABSTRACT

Constitutive activation of the EPO/JAK2 signaling cascade has recently been implicated in a variety of myeloproliferative disorders including polycythemia vera, essential thrombocythemia and myelofibrosis. In an effort to uncover therapeutic potential of blocking the EPO/JAK2 signaling cascade, we sought to discover selective inhibitors that block the kinase activity of JAK2. Herein, we describe the discovery and structure based optimization of a novel series of 2-amino-pyrazolo[1,5-a]pyrimidines that exhibit potent inhibition of JAK2.


Subject(s)
Janus Kinase 2/antagonists & inhibitors , Protein Kinase Inhibitors/pharmacology , Pyrazoles/pharmacology , Pyrimidines/pharmacology , Crystallography, X-Ray , Drug Discovery , Models, Molecular , Molecular Structure , Protein Kinase Inhibitors/chemical synthesis , Protein Kinase Inhibitors/chemistry , Pyrazoles/chemical synthesis , Pyrazoles/chemistry , Pyrimidines/chemical synthesis , Pyrimidines/chemistry , Signal Transduction/drug effects , Stereoisomerism , Structure-Activity Relationship
2.
Antimicrob Agents Chemother ; 50(3): 899-909, 2006 Mar.
Article in English | MEDLINE | ID: mdl-16495249

ABSTRACT

VX-950 is a potent, selective, peptidomimetic inhibitor of the hepatitis C virus (HCV) NS3-4A serine protease, and it demonstrated excellent antiviral activity both in genotype 1b HCV replicon cells (50% inhibitory concentration [IC50] = 354 nM) and in human fetal hepatocytes infected with genotype 1a HCV-positive patient sera (IC50 = 280 nM). VX-950 forms a covalent but reversible complex with the genotype 1a HCV NS3-4A protease in a slow-on, slow-off process with a steady-state inhibition constant (K(i)*) of 7 nM. Dissociation of the covalent enzyme-inhibitor complex of VX-950 and genotype 1a HCV protease has a half-life of almost an hour. A >4-log10 reduction in the HCV RNA levels was observed after a 2-week incubation of replicon cells with VX-950, with no rebound of viral RNA observed after withdrawal of the inhibitor. In several animal species, VX-950 exhibits a favorable pharmacokinetic profile with high exposure in the liver. In a recently developed HCV protease mouse model, VX-950 showed excellent inhibition of HCV NS3-4A protease activity in the liver. Therefore, the overall preclinical profile of VX-950 supports its candidacy as a novel oral therapy against hepatitis C.


Subject(s)
Hepacivirus/enzymology , Oligopeptides/pharmacology , Oligopeptides/pharmacokinetics , Serine Proteinase Inhibitors/pharmacology , Serine Proteinase Inhibitors/pharmacokinetics , Administration, Oral , Animals , Area Under Curve , Binding Sites , Biological Availability , Cell Line , Cells, Cultured , Dogs , Dose-Response Relationship, Drug , Drug Evaluation, Preclinical , Half-Life , Hepacivirus/drug effects , Hepatocytes/drug effects , Humans , Inhibitory Concentration 50 , Male , Mice , Mice, SCID , Oligopeptides/administration & dosage , RNA, Viral/physiology , Rats , Rats, Inbred F344 , Rats, Sprague-Dawley , Replicon/physiology , Serine Proteinase Inhibitors/administration & dosage , Substrate Specificity
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