Synthesis and biochemical studies of estrone sulfatase inhibitors.
The synthesis and biochemical evaluation of estrone sulfatase inhibitors are described. Inhibitors were designed through modifications of the substrate estrone sulfate. An in vitro assay using the microsomal fraction isolated from human term placenta was used to evaluate sulfatase inhibitory activity. All the inhibitors (except sulfonyl chloride analog) exhibited low inhibitory activities in the screening assay. Sulfonyl chloride analog is a strong inhibitor, which caused 91.5% inhibition of the enzymatic activity at 300 microM.
Li
P K
PK
Division of Medicinal Chemistry, Graduate School of Pharmaceutical Sciences, Duquesne University, Pittsburgh, PA 15282.
Pillai
R
R
Young
B L
BL
Bender
W H
WH
Martino
D M
DM
Lin
F T
FT
D004963:Estrenes / Q000138:chemical synthesis* / Q000494:pharmacology; D004970:Estrone / Q000031:analogs & derivatives* / Q000737:chemistry; D005260:Female; D006801:Humans; D008861:Microsomes / Q000201:enzymology; D015394:Molecular Structure; D010920:Placenta / Q000201:enzymology / Q000648:ultrastructure; D013429:Sulfatases / Q000037:antagonists & inhibitors*; D013450:Sulfones / Q000138:chemical synthesis* / Q000494:pharmacology
D004963:Estrenes; D013450:Sulfones; C080733:estra-1,3,5(10)-trien-17-one-3-sulfonyl chloride; D004970:Estrone; D013429:Sulfatases; C020121:estrone sulfatase; C017296:estrone sulfate