Yohimbine dimers exhibiting binding selectivities for human alpha2a- versus alpha2b-adrenergic receptors.
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.
Zheng
W
W
Department of Pharmaceutical Sciences, University of Tennessee, Memphis 38163, USA.
Lei
L
L
Lalchandani
S
S
Sun
G
G
Feller
D R
DR
Miller
D D
DD
D058669:Adrenergic alpha-2 Receptor Antagonists; D000317:Adrenergic alpha-Antagonists / Q000138:chemical synthesis / Q000737:chemistry / Q000494:pharmacology*; D000818:Animals; D001667:Binding, Competitive; D016466:CHO Cells; D006224:Cricetinae; D019281:Dimerization; D006801:Humans; D018341:Receptors, Adrenergic, alpha-2 / Q000235:genetics; D013329:Structure-Activity Relationship; D014162:Transfection; D015016:Yohimbine / Q000138:chemical synthesis / Q000737:chemistry / Q000494:pharmacology*
C547768:ADRA2A protein, human; C547771:ADRA2B protein, human; D058669:Adrenergic alpha-2 Receptor Antagonists; D000317:Adrenergic alpha-Antagonists; D018341:Receptors, Adrenergic, alpha-2; D015016:Yohimbine