Abstract
Starting from compound 1, a potent PI3Kα inhibitor having poor general kinase selectivity, we used structural data and modelling to identify key exploitable differences between PI3Kα and the other kinases. This approach led us to design chemical modifications of the central pyrazole, which solved the poor kinase selectivity seen as a strong liability for the initial compound 1. Amongst the modifications explored, a 1,3,4-triazole ring (as in compound 4) as a replacement of the initial pyrazole provided good potency against PI3Kα, with excellent kinase selectivity.
Keywords:
Kinase selectivity; PI3Kα inhibitor.
Copyright © 2015 Elsevier Ltd. All rights reserved.
MeSH terms
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Amino Acid Sequence
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Binding Sites
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Biomarkers, Tumor / antagonists & inhibitors
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Biomarkers, Tumor / chemistry
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Biomarkers, Tumor / genetics
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Cell Line, Tumor
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Class I Phosphatidylinositol 3-Kinases
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Drug Design
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Enzyme Inhibitors / chemical synthesis
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Enzyme Inhibitors / chemistry*
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Enzyme Inhibitors / pharmacology*
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Humans
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Models, Molecular
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Mutant Proteins / antagonists & inhibitors
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Mutant Proteins / chemistry
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Mutant Proteins / genetics
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Phosphatidylinositol 3-Kinases / chemistry
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Phosphatidylinositol 3-Kinases / genetics
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Phosphoinositide-3 Kinase Inhibitors*
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Pyrazoles / chemical synthesis
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Pyrazoles / chemistry
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Pyrazoles / pharmacology
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Structure-Activity Relationship
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Triazoles / chemical synthesis
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Triazoles / chemistry
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Triazoles / pharmacology
Substances
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Biomarkers, Tumor
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Enzyme Inhibitors
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Mutant Proteins
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Phosphoinositide-3 Kinase Inhibitors
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Pyrazoles
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Triazoles
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Class I Phosphatidylinositol 3-Kinases
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PIK3CA protein, human