Abstract
We report the discovery of a novel series of biaryl ethers as potent and selective PDE10A inhibitors. Structure-activity studies improved the potency and decreased Pgp-mediated efflux found in the initial compound 4. X-ray crystallographic studies revealed two novel binding modes to the catalytic site of the PDE10A enzyme.
Copyright © 2012 Elsevier Ltd. All rights reserved.
Publication types
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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ATP Binding Cassette Transporter, Subfamily B, Member 1 / metabolism*
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Crystallography, X-Ray
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Dose-Response Relationship, Drug
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Drug Discovery*
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Ethers / chemical synthesis
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Ethers / chemistry
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Ethers / metabolism*
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Ethers / pharmacology*
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Humans
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Models, Molecular
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Molecular Structure
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Phosphodiesterase Inhibitors / chemical synthesis
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Phosphodiesterase Inhibitors / chemistry
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Phosphodiesterase Inhibitors / metabolism*
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Phosphodiesterase Inhibitors / pharmacology*
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Phosphoric Diester Hydrolases / metabolism*
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Structure-Activity Relationship
Substances
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ATP Binding Cassette Transporter, Subfamily B, Member 1
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Ethers
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Phosphodiesterase Inhibitors
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PDE10A protein, human
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Phosphoric Diester Hydrolases