Abstract
In recent years, the investigation of acetylcholinesterase (AChE) inhibitors has gained further interest, because the involvement of the peripheral site of the enzyme in the beta-amyloid (Abeta) aggregation process has been disclosed. We present here, for the first time, a direct evidence of the Abeta antiaggregating action of an AChE inhibitor (AP2238) purposely designed to bind at both the catalytic and the peripheral sites of the human enzyme.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Acetylcholinesterase / chemistry*
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Acetylthiocholine / chemistry
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Alzheimer Disease / drug therapy
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Amyloid beta-Peptides / chemistry*
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Benzopyrans / chemical synthesis*
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Benzopyrans / chemistry
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Benzylamines / chemical synthesis*
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Benzylamines / chemistry
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Butyrylcholinesterase / chemistry
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Catalytic Domain
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Cholinesterase Inhibitors / chemical synthesis*
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Cholinesterase Inhibitors / chemistry
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Coumarins / chemical synthesis*
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Coumarins / chemistry
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Fluorometry
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Humans
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Hydrolysis
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Models, Molecular
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Structure-Activity Relationship
Substances
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AP 2238
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Amyloid beta-Peptides
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Benzopyrans
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Benzylamines
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Cholinesterase Inhibitors
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Coumarins
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Acetylthiocholine
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Acetylcholinesterase
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Butyrylcholinesterase