152904-82-0

Basic information

• Product Name: Carbamic acid, [(diphenoxyphosphinyl)(4-nitrophenyl)methyl]-, phenylmethyl ester
• CAS NO: 152904-82-0
• Molecular Formula: C27H23N2O7P
• Molecular Weight: 518.463
• Mol File: 152904-82-0.mol

Chemical Properties

• CAS DataBase Reference: Carbamic acid, [(diphenoxyphosphinyl)(4-nitrophenyl)methyl]-, phenylmethyl ester(CAS DataBase Reference)
• NIST Chemistry Reference: Carbamic acid, [(diphenoxyphosphinyl)(4-nitrophenyl)methyl]-, phenylmethyl ester(152904-82-0)
• EPA Substance Registry System: Carbamic acid, [(diphenoxyphosphinyl)(4-nitrophenyl)methyl]-, phenylmethyl ester(152904-82-0)

Safety Data

• Hazardous Substances Data: 152904-82-0(Hazardous Substances Data)

Upstream product

• 621-84-1 O-benzyl carbamate 
• 4712-55-4 diphenyl hydrogen phosphite 
• 555-16-8 4-nitrobenzaldehdye 
• 101-02-0 triphenyl phosphite 

Downstream Products

• 785827-88-5 diphenyl α-N-(benzyloxycarbonyl)amino(4-aminophenyl)methanephosphonate 
• 174298-45-4 C₁₉H₁₇N₂O₅P*BrH 
• 1403781-80-5 diphenyl (isothiocyanato(4-nitrophenyl)methyl)phosphonate 
• 1450636-19-7 diphenyl α-N-(propiolamido)-(4-nitro-phenyl)methanephosphonate 
• 1450636-20-0 diphenyl α-N-(propiolamido)-(4-amino-phenyl)methanephosphonate 
• 1450636-21-1 diphenyl α-N-(propiolamido)(4-guanidiniumphenyl)methanephosphonate 

Relevant articles and documents

A Fluorescent-Labeled Phosphono Bisbenzguanidine As an Activity-Based Probe for Matriptase

Activity-based probes are compounds that exclusively form covalent bonds with active enzymes. They can be utilized to profile enzyme activities in vivo, to identify target enzymes and to characterize their function. The design of a new activity-based probe for matriptase, a member of the type II transmembrane serine proteases, is based on linker-connected bis-benzguanidines. An amino acid, introduced as linker, bears the coumarin fluorophore. Moreover, an incorporated phosphonate allows for a covalent interaction with the active-site serine. The resulting irreversible mode of action was demonstrated, leading to enzyme inactivation and, simultaneously, to a fluorescence labeling of matriptase. The ten-step synthetic approach to a coumarin-labeled bis-benzguanidine and its evaluation as activity-based probe for matriptase based on in-gel fluorescence and fluorescence HPLC is reported. HPLC fluorescence detection as a new application for activity-based probes for proteases is demonstrated herein for the first time.

One-pot synthesis of α-aminophosphonates by yttrium-catalyzed Birum-Oleksyszyn reaction

For the first time, yttrium triflate was used as an efficient green catalyst for the synthesis of α-aminophosphonates through a one-pot three-component Birum-Oleksyszyn reaction. Under the action of this Lewis acid, enhancement of the yield and reaction c

A Suite of Activity-Based Probes to Dissect the KLK Activome in Drug-Resistant Prostate Cancer

Kallikrein-related peptidases (KLKs) are a family of secreted serine proteases, which form a network (the KLK activome) with an important role in proteolysis and signaling. In prostate cancer (PCa), increased KLK activity promotes tumor growth and metastasis through multiple biochemical pathways, and specific quantification and tracking of changes in the KLK activome could contribute to validation of KLKs as potential drug targets. Herein we report a technology platform based on novel activity-based probes (ABPs) and inhibitors enabling simultaneous orthogonal analysis of KLK2, KLK3, and KLK14 activity in hormone-responsive PCa cell lines and tumor homogenates. Importantly, we identifed a significant decoupling of KLK activity and abundance and suggest that KLK proteolysis should be considered as an additional parameter, along with the PSA blood test, for accurate PCa diagnosis and monitoring. Using selective inhibitors and multiplexed fluorescent activity-based protein profiling (ABPP), we dissect the KLK activome in PCa cells and show that increased KLK14 activity leads to a migratory phenotype. Furthermore, using biotinylated ABPs, we show that active KLK molecules are secreted into the bone microenvironment by PCa cells following stimulation by osteoblasts suggesting KLK-mediated signaling mechanisms could contribute to PCa metastasis to bone. Together our findings show that ABPP is a powerful approach to dissect dysregulation of the KLK activome as a promising and previously underappreciated therapeutic target in advanced PCa.

α-Amino Diphenyl Phosphonates as Novel Inhibitors of Escherichia coli ClpP Protease

Increased Gram-negative bacteria resistance to antibiotics is becoming a global problem, and new classes of antibiotics with novel mechanisms of action are required. The caseinolytic protease subunit P (ClpP) is a serine protease conserved among bacteria that is considered as an interesting drug target. ClpP function is involved in protein turnover and homeostasis, stress response, and virulence among other processes. The focus of this study was to identify new inhibitors of Escherichia coli ClpP and to understand their mode of action. A focused library of serine protease inhibitors based on diaryl phosphonate warheads was tested for ClpP inhibition, and a chemical exploration around the hit compounds was conducted. Altogether, 14 new potent inhibitors of E. coli ClpP were identified. Compounds 85 and 92 emerged as most interesting compounds from this study due to their potency and, respectively, to its moderate but consistent antibacterial properties as well as the favorable cytotoxicity profile.

Phosphono Bisbenzguanidines as Irreversible Dipeptidomimetic Inhibitors and Activity-Based Probes of Matriptase-2

Matriptase-2, a type II transmembrane serine protease, plays a key role in human iron homeostasis. Inhibition of matriptase-2 is considered as an attractive strategy for the treatment of iron-overload diseases, such as hemochromatosis and β-thalassemia. In the present study, synthetic routes to nine dipeptidomimetic inactivators were developed. Five active compounds (41–45) were identified and characterized kinetically as irreversible inhibitors of matriptase-2. In addition to a phosphonate warhead, these dipeptides possess two benzguanidine moieties as arginine mimetics to provide affinity for matriptase-2 by binding to the S1 and S3/S4 subpockets, respectively. This binding mode was strongly supported by covalent docking analysis. Compounds 41–45 were obtained as mixtures of two diastereomers and were therefore separated into the single epimers. Compound 45 A, with S configuration at the N-terminal amino acid and R configuration at the phosphonate carbon atom, was the most potent matriptase-2 inactivator with a rate constant of inactivation of 2790 m?1s?1and abolished the activity of membrane-bound matriptase-2 on the surface of intact cells. Based on the chemotyp of phosphono bisbenzguanidines, the design and synthesis of a fluorescent probe (51 A) by insertion of a coumarin label is described. The in-gel fluorescence detection of matriptase-2 was demonstrated by applying 51 A as the first activity-based probe for this enzyme.

NOVEL AMINOALKYLPHOSPHONATE COMPOUNDS AND METHODS USING SAME

The present invention includes aminoalkylphosphonate compounds that are useful in preventing and/or treating prostate cancer in a male subject. The present invention further includes methods of preventing and/or treating prostate cancer in a male subject

Synthesis of fluorescent (benzyloxycarbonylamino)(aryl)methylphosphonates

The synthesis of a library of structurally variable aromatic esters of (benzyloxycarbonylamino)(aryl)methylphosphonic acids is described by means of the Oleksyszyn reaction. The library was enlarged by the application of a Suzuki-Miayra approach and by preparation of mixed esters.

Tuning activity-based probe selectivity for serine proteases by on-resin 'click' construction of peptide diphenyl phosphonates

Activity-based probes (ABPs) are powerful tools for functional proteomics studies. Their selectivity can be influenced by modification of a recognition element that interacts with pockets near the active site. For serine proteases there are a limited numb

Convenient syntheses of novel 1-isothiocyano-alkylphosphonate diphenyl ester derivatives with potential biological activity

Herein, we describe a convenient method for the syntheses of novel 1-isothiocyano-alkylphosphonate diaryl ester derivatives and their antiproliferative activity. The syntheses are based on dithiocarbamates obtained in situ with the use of carbon disulfide

New potent cathepsin G phosphonate inhibitors

Cathepsin G is an enzyme with dual chymotrypsin and trypsin-like specificity. As a leukocyte proteinase it is involved in the early stages of the immune response. In this work the synthesis and inhibitory activity of diaryl phosphonic-type irreversible ca