Abstract
A potent and selective inhibitor of KCNQ2, (S)-5 (ML252, IC(50) = 69 nM), was discovered after a high-throughput screen of the MLPCN library was performed. SAR studies revealed a small structural change (ethyl group to hydrogen) caused a functional shift from antagonist to agonist activity (37, EC(50) = 170 nM), suggesting an interaction at a critical site for controlling gating of KCNQ2 channels.
Publication types
-
Research Support, N.I.H., Extramural
MeSH terms
-
Animals
-
Brain / metabolism*
-
Databases, Factual
-
High-Throughput Screening Assays
-
Humans
-
KCNQ2 Potassium Channel / antagonists & inhibitors*
-
KCNQ2 Potassium Channel / chemistry
-
Microsomes, Liver / metabolism
-
Permeability
-
Phenylbutyrates / chemical synthesis*
-
Phenylbutyrates / chemistry
-
Phenylbutyrates / pharmacokinetics
-
Potassium Channel Blockers / chemical synthesis*
-
Potassium Channel Blockers / chemistry
-
Potassium Channel Blockers / pharmacokinetics
-
Pyrrolidines / chemical synthesis*
-
Pyrrolidines / chemistry
-
Pyrrolidines / pharmacokinetics
-
Rats
-
Small Molecule Libraries
-
Stereoisomerism
-
Structure-Activity Relationship
Substances
-
2-phenyl-N-(2-(pyrrolidin-1-yl)phenyl)butanamide
-
KCNQ2 Potassium Channel
-
Phenylbutyrates
-
Potassium Channel Blockers
-
Pyrrolidines
-
Small Molecule Libraries