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2685-03-2

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2685-03-2 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 2685-03-2 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 2,6,8 and 5 respectively; the second part has 2 digits, 0 and 3 respectively.
Calculate Digit Verification of CAS Registry Number 2685-03:
(6*2)+(5*6)+(4*8)+(3*5)+(2*0)+(1*3)=92
92 % 10 = 2
So 2685-03-2 is a valid CAS Registry Number.

2685-03-2Downstream Products

2685-03-2Relevant articles and documents

Stereochemical probes for the estrogen receptor: Synthesis and receptor binding of (17α,20E/Z)-21-phenyl-19-norpregna-1,3,5(10),20-tetraene-3,17β- diols

Hanson, Robert N.,Herman, Lee W.,Fiaschi, Rita,Napolitano, Elio

, p. 718 - 722 (1996)

Previous studies from our laboratory using 17α-E and 17α-Z-halovinyl and phenylthiovinyl estradiols demonstrated a marked preference for the Z stereochemistry and a significant steric tolerance for the Z-vinyl substituent. To further explore the extent of

Structure-activity relationships of 17α-derivatives of estradiol as inhibitors of steroid sulfatase

Boivin,Luu-The,Lachance,Labrie,Poirier

, p. 4465 - 4478 (2007/10/03)

The steroid sulfatase or steryl sulfatase is a microsomal enzyme widely distributed in human tissues that catalyzes the hydrolysis of sulfated 3-hydroxy steroids to the corresponding free active 3-hydroxy steroids. Since androgens and estrogens may be synthesized inside the cancerous cells starting from dehydroepiandrosterone sulfate (DHEAS) and estrone sulfate (E1S) available in blood circulation, the use of therapeutic agents that inhibit steroid sulfatase activity may be a rewarding approach to the treatment of androgeno-sensitive and estrogeno-sensitive diseases. In the present study, we report the chemical synthesis and biological evaluation of a new family of steroid sulfatase inhibitors. The inhibitors were designed by adding an alkyl, a phenyl, a benzyl, or a benzyl substituted at position 17α of estradiol (E2), a C18-steroid, and enzymatic assays were performed using the steroid sulfatase of homogenized JEG-3 cells or transfected in HEK-293 cells. We observed that a hydrophobic substituent induces powerful inhibition of steroid sulfatase while a hydrophilic one was weak. Although a hydrophobic group at the 17α-position increased the inhibitory activity, the steric factors contribute to the opposite effect. As exemplified by 17α-decyl-E2 and 17α-dodecyl-E2, a long flexible side chain prevents adequate fitting into the enzyme catalytic site, thus decreasing capacity to inhibit the steroid sulfatase activity. In the alkyl series, the best compromise between hydrophobicity and steric hindrance was obtained with the octyl group (IC50 = 440 nM), but judicious branching of side chain could improve this further. Benzyl substituted derivatives of estradiol were better inhibitors than alkyl analogues. Among the series of 17α-(benzyl substituted)-E2 derivatives studied, the 3′-bromobenzyl, 4′-tert-butylbenzyl, 4′-butylbenzyl, and 4′-benzyloxybenzyl groups provided the most potent inhibition of steroid sulfatase transformation of E1S into E1 (IC50 = 24, 28, 25, and 22 nM, respectively). As an example, the tert-butylbenzyl group increases the ability of the E2 nucleus to inhibit the steroid sulfatase by 3000-fold, and it also inhibits similarly the steroid sulfatase transformations of both natural substrates, E1S and DHEAS. Interestingly, the newly reported family of steroid sulfatase inhibitors acts by a reversible mechanism of action that is different from the irreversible mechanism of the known inhibitor estrone sulfamate (EMATE).

17α -Substituted analogs of estradiol for the development of fluorescent estrogen receptor ligands

Salman, Mohammad,Reddy,Delgado, Pete,Stotterl, Philip L.,Fulcher, Letitia C.,Chamness, Gary C.

, p. 375 - 387 (2007/10/02)

For the successful development of a high-affinity fluorophore-estradiol conjugate, the fluorophore must be attached to the estradiol molecule at a position that interferes least with its binding to the receptor. We have concentrated on 17α. substituents as models for fluorophore attachment, based on literature precedent and on our earlier work with small 17α. side chains. In this report, we describe syntheses and estrogen receptor binding affinities of 19 analogs of estradiol substituted in the 17α position with larger side chains (of six to 11 carbons), some of which may be synthetically modified to link a fluorophore. These analogs were synthesized either by nucleophilic cleavage of estrone-17β-oxirane 3-benzyl ether and subsequent debenzylation (4 to 18), by cross-coupling of alkynes (21 to 24), by alkylation of 17 αethynylestradiol 3,17-bis(tetrahydropyranyl ether) and subsequent acidic hydrolysis (25 to 28), or by reacting estrone either with appropriate aryllalkynyllithium reagents (29,30, and 32) or with benzylmagnesium bromide (31). Relative binding affinities of these newly synthesized analogs were determined for estrogen receptor (rat uterus) using a standard competition assay. The results suggest that analogs with reduced mobility and/or more polarizable electron density in the side chain generally bind more strongly to the receptor. The relative affinities of several selected compounds were also determined in the presence of 4% dimethylformamide; some compounds bearing larger, nonpolar 17α. substituents showed dramatically improved affinities, while affinities for compounds with shorter nonpolar side chains remained largely unchanged. These binding affinity results should be useful in designing new high-affinity fluorescent ligands for the estrogen receptor.

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