Synthesis and binding affinity to human alpha and beta estrogen receptors of various 7-hydroxycoumarins substituted at 4- and 3,4- positions.
The study of the relative binding affinity (RBA) to the human alpha and beta estrogen receptors (ERs) of various 7-hydroxycoumarins substituted at 4- and 3,4- positions is weak and lacks in selectivity for both ERalpha and ERbeta. The 4-(4-hydroxyphenyl)-7-hydroxycoumarin shows a weak RBA to ERbeta and 3,4-diphenyl-7-hydroxycoumarin presents a stronger RBA to ERalpha than ERbeta.
Kirkiacharian
Serge
S
Faculté de Pharmacie de Paris-Sud, Laboratoire de Chimie Thérapeutique, 5 rue Jean-Baptiste-Clément, 92296 Chatenay Malabry cedex, France. serge.kirkiacharian@cep.u-psud.fr
Lormier
Anh Tuan
AT
Chidiack
Henri
H
Bouchoux
Françoise
F
Cérède
Evelyne
E
D000818:Animals; D019556:COS Cells; D002522:Chlorocebus aethiops; D047628:Estrogen Receptor alpha / Q000378:metabolism*; D047629:Estrogen Receptor beta / Q000378:metabolism*; D006801:Humans; D011485:Protein Binding / Q000502:physiology; D014468:Umbelliferones / Q000138:chemical synthesis* / Q000378:metabolism*
D047628:Estrogen Receptor alpha; D047629:Estrogen Receptor beta; D014468:Umbelliferones