Abstract
Modifications to the basic side-chain of early lead structures of the indolyl quinolinone class of KDR kinase inhibitors resulted in improved pharmacokinetic and ancillary profiles. Specifically, compounds bearing 5-amido- and 5-sulphonamido-indolyl substituents exhibited lower plasma clearance and weaker binding affinity for the I(Kr) potassium channel hERG.
MeSH terms
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Animals
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Cation Transport Proteins / metabolism*
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Cell Line
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Dogs
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Enzyme Inhibitors / chemistry
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Enzyme Inhibitors / pharmacokinetics*
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Ether-A-Go-Go Potassium Channels
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Humans
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Microsomes, Liver / enzymology
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Potassium Channels / metabolism*
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Potassium Channels, Voltage-Gated*
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Protein Binding / physiology
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Quinolones / chemistry
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Quinolones / pharmacokinetics*
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Rats
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Vascular Endothelial Growth Factor Receptor-2 / antagonists & inhibitors*
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Vascular Endothelial Growth Factor Receptor-2 / metabolism
Substances
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Cation Transport Proteins
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Enzyme Inhibitors
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Ether-A-Go-Go Potassium Channels
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KCNH6 protein, human
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Potassium Channels
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Potassium Channels, Voltage-Gated
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Quinolones
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Vascular Endothelial Growth Factor Receptor-2