Abstract
A series of yohimbine dimers was prepared and evaluated at the human alpha2a- and alpha2b-adrenergic receptors (ARs) expressed in Chinese hamster ovary (CHO) cells. All dimers display higher binding selectivities for alpha2a versus alpha2b subtype than yohimbine, and four compounds (3d, 3e, 3g and 3i) represent the most potent and alpha2a versus alpha2b-AR selective ligands identified so far.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Adrenergic alpha-2 Receptor Antagonists*
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Adrenergic alpha-Antagonists / chemical synthesis
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Adrenergic alpha-Antagonists / chemistry
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Adrenergic alpha-Antagonists / pharmacology*
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Animals
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Binding, Competitive
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CHO Cells
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Cricetinae
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Dimerization
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Humans
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Receptors, Adrenergic, alpha-2 / genetics
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Structure-Activity Relationship
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Transfection
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Yohimbine / chemical synthesis
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Yohimbine / chemistry
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Yohimbine / pharmacology*
Substances
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ADRA2A protein, human
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ADRA2B protein, human
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Adrenergic alpha-2 Receptor Antagonists
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Adrenergic alpha-Antagonists
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Receptors, Adrenergic, alpha-2
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Yohimbine