Abstract
A series of hybrid molecules containing the cyclopropylmethylamino side chain found in homotryptamine (1S,2S)-2c and an isosteric heteroaryl or naphthyl core were prepared and their binding affinities for the human serotonin transporter determined. The most potent isosteres were CN-substituted naphthalenes. These results demonstrate that isosteric aromatic cores which lack an H-bond donor site may be substituted for the indole nucleus without substantial loss in hSERT binding.
MeSH terms
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Dopamine Plasma Membrane Transport Proteins / antagonists & inhibitors
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Dopamine Plasma Membrane Transport Proteins / metabolism
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Heterocyclic Compounds / chemical synthesis
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Heterocyclic Compounds / chemistry*
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Heterocyclic Compounds / pharmacology*
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Humans
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Inhibitory Concentration 50
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Molecular Conformation
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Norepinephrine Plasma Membrane Transport Proteins / antagonists & inhibitors
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Norepinephrine Plasma Membrane Transport Proteins / metabolism
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Selective Serotonin Reuptake Inhibitors / chemical synthesis
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Selective Serotonin Reuptake Inhibitors / chemistry*
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Selective Serotonin Reuptake Inhibitors / pharmacology*
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Structure-Activity Relationship
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Tryptamines / chemistry*
Substances
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Dopamine Plasma Membrane Transport Proteins
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Heterocyclic Compounds
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Norepinephrine Plasma Membrane Transport Proteins
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Serotonin Uptake Inhibitors
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Tryptamines
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tryptamine