Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 4 de 4
Filter
Add more filters

Database
Language
Publication year range
1.
Bioorg Med Chem Lett ; 26(19): 4606-4612, 2016 10 01.
Article in English | MEDLINE | ID: mdl-27578246

ABSTRACT

The optimisation of the azanaphthyridine series of Spleen Tyrosine Kinase inhibitors is described. The medicinal chemistry strategy was focused on optimising the human whole blood activity whilst achieving a sufficient margin over hERG activity. A good pharmacokinetic profile was achieved by modification of the pKa. Morpholine compound 32 is a potent SYK inhibitor showing moderate selectivity, good oral bioavailability and good efficacy in the rat Arthus model but demonstrated a genotoxic potential in the Ames assay.


Subject(s)
Naphthyridines/pharmacology , Protein Kinase Inhibitors/pharmacology , Administration, Oral , Animals , Biological Availability , Crystallography, X-Ray , Humans , Mutagenicity Tests , Naphthyridines/administration & dosage , Naphthyridines/pharmacokinetics , Protein Kinase Inhibitors/administration & dosage , Protein Kinase Inhibitors/pharmacokinetics , Rats , Structure-Activity Relationship
2.
Bioorg Med Chem Lett ; 21(20): 6188-94, 2011 Oct 15.
Article in English | MEDLINE | ID: mdl-21903390
3.
ACS Chem Biol ; 11(7): 2002-10, 2016 07 15.
Article in English | MEDLINE | ID: mdl-27197014

ABSTRACT

The 2-oxoglutarate-dependent dioxygenase target class comprises around 60 enzymes including several subfamilies with relevance to human disease, such as the prolyl hydroxylases and the Jumonji-type lysine demethylases. Current drug discovery approaches are largely based on small molecule inhibitors targeting the iron/2-oxoglutarate cofactor binding site. We have devised a chemoproteomics approach based on a combination of unselective active-site ligands tethered to beads, enabling affinity capturing of around 40 different dioxygenase enzymes from human cells. Mass-spectrometry-based quantification of bead-bound enzymes using a free-ligand competition-binding format enabled the comprehensive determination of affinities for the cosubstrate 2-oxoglutarate and for oncometabolites such as 2-hydroxyglutarate. We also profiled a set of representative drug-like inhibitor compounds. The results indicate that intracellular competition by endogenous cofactors and high active site similarity present substantial challenges for drug discovery for this target class.


Subject(s)
Dioxygenases/metabolism , Ketoglutaric Acids/metabolism , Proteomics
SELECTION OF CITATIONS
SEARCH DETAIL