114865-17-7 Usage
Description
(9H-fluoren-9-yl)methyl 4-hydroxyphenethylcarbamate is a carbamate compound characterized by the presence of a fluorenyl group and a 4-hydroxyphenethyl group. This molecule is known for its stability and rigidity, which makes it a valuable scaffold for drug design and discovery. The 4-hydroxyphenethyl group in the molecule suggests potential biological activity, as phenethyl compounds are recognized for their diverse pharmacological properties.
Uses
Used in Organic Synthesis:
(9H-fluoren-9-yl)methyl 4-hydroxyphenethylcarbamate is used as a building block in organic synthesis for the creation of various compounds, including potential drug candidates. The unique structure of the molecule, with its fluorenyl and 4-hydroxyphenethyl groups, allows for the development of a wide range of chemical products.
Used in Pharmaceutical Research:
In the pharmaceutical industry, (9H-fluoren-9-yl)methyl 4-hydroxyphenethylcarbamate is used as a key component in the synthesis of new drug candidates. (9H-fluoren-9-yl)methyl 4-hydroxyphenethylcarbamate's potential biological activity, stemming from its 4-hydroxyphenethyl group, makes it a promising starting point for the development of novel medications with various therapeutic applications.
Used in Medicinal Chemistry:
(9H-fluoren-9-yl)methyl 4-hydroxyphenethylcarbamate is utilized in medicinal chemistry as a versatile compound with potential applications in drug development. Its structural features, including the fluorenyl group, contribute to its stability and make it an attractive scaffold for the design of new therapeutic agents.
Overall, (9H-fluoren-9-yl)methyl 4-hydroxyphenethylcarbamate is a compound with significant potential in various fields, including organic synthesis, pharmaceutical research, and medicinal chemistry, due to its unique structural properties and potential biological activity.
Check Digit Verification of cas no
The CAS Registry Mumber 114865-17-7 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 1,1,4,8,6 and 5 respectively; the second part has 2 digits, 1 and 7 respectively.
Calculate Digit Verification of CAS Registry Number 114865-17:
(8*1)+(7*1)+(6*4)+(5*8)+(4*6)+(3*5)+(2*1)+(1*7)=127
127 % 10 = 7
So 114865-17-7 is a valid CAS Registry Number.
114865-17-7Relevant articles and documents
Toward a mechanism-based fluorescent assay for site-specific recombinases and topoisomerases: Assay design and syntheses of fluorescent substrates
Panigrahi, Gagan,Zhao, Bao-Ping,Krepinsky, Jiri J.,Sadowski, Paul D.
, p. 12004 - 12011 (1996)
Site-specific recombinases and topoisomerases break and rejoin the phosphodiester bonds of DNA. Both classes of enzymes do so through the formation of a covalent intermediate involving a phosphodiester bond with a hydroxylated amino acid (usually tyrosine
Beyond Basicity: Discovery of Nonbasic DENV-2 Protease Inhibitors with Potent Activity in Cell Culture
Kühl, Nikos,Leuthold, Mila M.,Behnam, Mira A. M.,Klein, Christian D.
supporting information, p. 4567 - 4587 (2021/05/06)
The viral serine protease NS2B-NS3 is one of the promising targets for drug discovery against dengue virus and other flaviviruses. The molecular recognition preferences of the protease favor basic, positively charged moieties as substrates and inhibitors, which leads to pharmacokinetic liabilities and off-target interactions with host proteases such as thrombin. We here present the results of efforts that were aimed specifically at the discovery and development of noncharged, small-molecular inhibitors of the flaviviral proteases. A key factor in the discovery of these compounds was a cellular reporter gene assay for the dengue protease, the DENV2proHeLa system. Extensive structure-activity relationship explorations resulted in novel benzamide derivatives with submicromolar activities in viral replication assays (EC50 0.24 μM), selectivity against off-target proteases, and negligible cytotoxicity. This structural class has increased drug-likeness compared to most of the previously published active-site-directed flaviviral protease inhibitors and includes promising candidates for further preclinical development.
