Abstract
Pyrrolylquinoxalinediones carrying aminoalkyl residues were evaluated for affinity to the recombinant, homomeric kainate receptors GluR5, GluR6 and GluR7. Most derivatives preferred binding to GluR5. In particular, the piperazine 6e represents a highly potent and selective antagonist to GluR5.
MeSH terms
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Animals
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Binding Sites
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Dose-Response Relationship, Drug
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Excitatory Amino Acid Antagonists / chemical synthesis
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Excitatory Amino Acid Antagonists / chemistry
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Excitatory Amino Acid Antagonists / metabolism
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Excitatory Amino Acid Antagonists / pharmacology
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Ligands
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Mice
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Molecular Structure
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N-Methylaspartate / pharmacology
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Piperazines / chemical synthesis
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Piperazines / chemistry*
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Piperazines / metabolism*
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Piperazines / pharmacology
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Quinoxalines / chemical synthesis
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Quinoxalines / chemistry*
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Quinoxalines / metabolism*
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Quinoxalines / pharmacology
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Receptors, Kainic Acid / antagonists & inhibitors
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Receptors, Kainic Acid / chemistry
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Receptors, Kainic Acid / metabolism*
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Seizures / chemically induced
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Seizures / drug therapy
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Structure-Activity Relationship
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Substrate Specificity
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alpha-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid / pharmacology
Substances
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Excitatory Amino Acid Antagonists
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Gluk1 kainate receptor
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Ligands
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Piperazines
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Quinoxalines
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Receptors, Kainic Acid
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N-Methylaspartate
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alpha-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid