22074-14-2

Upstream product

• 555-21-5 4-Nitrophenylacetonitrile 
• 95-01-2 2,4-Dihydroxybenzaldehyde 
• 104-03-0 4-nitrobenzeneacetic acid 
• 50434-36-1 4-nitrophenylacetyl chloride 

Downstream Products

• 66267-85-4 3-(4-aminophenyl)-7-hydroxy-2H-chromen-2-one 

Relevant academic research and scientific papers

Synthesis and steroid sulfatase inhibitory activities of: N -phosphorylated 3-(4-aminophenyl)-coumarin-7-O-sulfamates

In the present work, we report convenient methods for the synthesis and biological evaluation of N-phosphorylated derivatives of 3-(4-aminophenyl)-coumarin-7-O-sulfamate as potential steroid sulfatase (STS) inhibitors. Their binding modes were modeled using docking techniques. The inhibitory effects of the synthesized compounds were tested on STS isolated from human placenta. All of the newly synthesised coumarin derivatives were powerful inhibitors of STS with IC50 values ranging between 0.19 and 0.78 μM. In particular, we found that 3-[4-(diphenoxy-phosphorylamino)-phenyl]-coumarin-7-O-sulfamate 10e and 3-[4-(dibenzyloxy-phosphorylamino)-phenyl]-coumarin-7-O-sulfamate 10f produced the highest inhibitory effects, with IC50 values of 0.19 and 0.24 μM, respectively (IC50 values of 1.38 μM for coumarin-7-O-sulfamate 2 and 1.03 μM for coumate 3 used as reference). The structure-activity relationships of the synthesized coumarin derivatives toward the STS enzyme were discussed.

Synthesis and biological evaluation of fluorinated N-benzoyl and N-phenylacetoyl derivatives of 3-(4-aminophenyl)-coumarin-7-O-sulfamate as steroid sulfatase inhibitors

In the present work, we report convenient methods for the synthesis of 3-(4-aminophenyl)-coumarin-7-O-sulfamate derivatives N-acylated with fluorinated analogues of benzoic or phenylacetic acid as steroid sulfatase (STS) inhibitors. The design of these potential STS inhibitors was supported by molecular modeling techniques. Additionally, computational docking methods were used to determine the binding modes of the synthesized inhibitors and to identify potential interactions between inhibitors and amino acid residues located in the active site of STS. The inhibitory effects of the synthesized compounds were tested on STS isolated from human placenta and against estrogen receptor-(ER)-positive MCF-7 and T47D cells, as well as ER-negative MDA-MB-231 and SkBr3 cancer cell lines. In the course of our investigation, compounds 6c and 6j demonstrated the highest inhibitory effect in enzymatic STS assays, both with IC50values of 0.18?μM (the IC50value of coumarin-7-O-sulfamate is 1.38?μM, used as a reference). Compound 6j exhibited the highest potency against the MCF-7 and T47D cell lines (15.9?μM and 8.7?μM, respectively). The GI50values of tamoxifen (used as a reference) were 6.8; 10.6; 15.1; 12.5?μM against MCF-7, T47D, MDA-MB-231 and SkBr3 cancer cell lines, respectively. Despite the slightly lower activity of compounds 1 and 2 (both in enzymatic and cell-based experiments) compared to 6g and 6j, analogues 1 and 2 proved to selectively inhibit the growth of ER- and PR-positive cell lines.

FLUORESCENT PROBES FOR ABASIC SITE DETECTION

A fluorescent probe for binding to and detection of AP sites of DNA includes the following formula: F-L-X where F is a fluorescent moiety, X is an aminooxy group (-ONH2), and L is a linker that links or couples the fluorescent moiety to the oxy

Synthesis and binding affinity of 3-aryl-7-hydroxycoumarins to human α and β estrogen receptors

The synthesis of a set of substituted 3-aryl-7-hydroxycoumarins was performed. The study of the relations between their structure and their relative binding affinity (RBA) to human α and β estrogen receptors was achieved.