132372-69-1

Basic information

• Product Name: diphenyl α-N-(benzyloxycarbonyl)amino-2-phenylethylphosphonate
• CAS NO: 132372-69-1
• Molecular Weight: 487.492
• Mol File: 132372-69-1.mol

Chemical Properties

• CAS DataBase Reference: diphenyl α-N-(benzyloxycarbonyl)amino-2-phenylethylphosphonate(CAS DataBase Reference)
• NIST Chemistry Reference: diphenyl α-N-(benzyloxycarbonyl)amino-2-phenylethylphosphonate(132372-69-1)
• EPA Substance Registry System: diphenyl α-N-(benzyloxycarbonyl)amino-2-phenylethylphosphonate(132372-69-1)

Safety Data

• Hazardous Substances Data: 132372-69-1(Hazardous Substances Data)

Upstream product

• 101-02-0 triphenyl phosphite 
• 621-84-1 O-benzyl carbamate 
• 122-78-1 phenylacetaldehyde 
• 501-53-1 benzyl chloroformate 
• 115-86-6 phosphoric acid triphenyl ester 

Downstream Products

• 84690-42-6 dimethyl 1-benzyloxycarbonylamino-2-phenylethyl phosphonate 
• 73270-44-7 diphenyl (1-amino-2-phenyl)ethylphosphonate 
• 901773-71-5 (1-formylamino-2-phenyl-ethyl)-phosphonic acid diphenyl ester 
• 107072-64-0 methyl <1--2-phenylethyl>phosphonate 
• 109638-82-6 C₁₇H₁₉ClNO₄P 
• 109638-81-5 (1-amino-2-phenylethyl)phosphonic acid, dimethyl ester 
• 109638-91-7 (2S)-2-<oxy>-4-methylpentanoate 
• 109638-95-1 (S)-2-[(1-Benzyloxycarbonylamino-2-phenyl-ethyl)-hydroxy-phosphinoyloxy]-4-methyl-pentanoic acid 
• 109638-84-8 methyl (2S)-2-<amino>ethyl>phosphinyl>oxy>-4-methylpentanoate 
• 1450636-18-6 diphenyl α-N-(propiolamido)-2-phenylethylphosphonate 
• 107072-80-0 diethyl 1?(N?benzyloxycarbonylamino)?2?phenylethylphosphonate 

Relevant articles and documents

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

Selective removal of chymotrypsin using diphenyl α- aminoalkylphosphonate immobilized on Sepharose gel

A diphenyl α-aminoalkylphosphonate derivative, which is an irreversible inhibitor of chymotrypsin-like serine proteases, was immobilized on cyanogen bromide-activated Sepharose, and the selective binding of chymotrypsin to the obtained inhibitor-gel was evaluated using batch and column methods. Complete removal of chymotrypsin in an aqueous solution was done using the column method, while partial removal was done using the batch method.

Generation of a quenched phosphonate activity-based probe for labelling the active KLK7 protease

Kallikrein 7 (KLK7) is a chymotrypsin-like serine protease with established roles in skin diseases like the rare Netherton syndrome, an overdesquamating and inflammatory condition, but also common atopic dermatitis, and a potential drug target for these a

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

Direct18F-Labeling of Biomolecules via Spontaneous Site-Specific Nucleophilic Substitution by F-on Phosphonate Prostheses

We describe a high radiochemical yield late-stage direct 18F-labeling of bare biomolecules containing common active groups. Spontaneity and site-selectivity are attributed to the remarkably higher rates of nucleophilic substitution reactions on phosphonates than on other electrophiles by F- at various hydrogen bond forms. Rapid access to many medicinally significant 18F-labeled biomolecules is achieved at 21-68% radiochemical yields and 35.9-55.1 GBq μmol-1 molar activities both manually or automatically.

A novel theranostic activity-based probe targeting kallikrein 7 for the diagnosis and treatment of skin diseases

We applied a newin silicoapproach for using protease-substrate motifs to design a kallikrein 7 (KLK7)-specific phosphonate activity-based probe (ABP) to quantify the active KLK7in situ. Epidermal application of the ABP-inhibitor onSpink5?/?Klk5

Structure-based design, synthesis, and evaluation of the biological activity of novel phosphoroorganic small molecule IAP antagonists

One of the strategies employed by novel anticancer therapies is to put the process of apoptosis back on track by blocking the interaction between inhibitor of apoptosis proteins (IAPs) and caspases. The activity of caspases is modulated by the caspases themselves in a caspase/procaspase proteolytic cascade and by their interaction with IAPs. Caspases can be released from the inhibitory influence of IAPs by proapoptotic proteins such as secondary mitochondrial activator of caspases (Smac) that share an IAP binding motif (IBM). The main purpose of the present study was the design and synthesis of phosphorus-based peptidyl antagonists of IAPs that mimic the endogenous Smac protein, which blocks the interaction between IAPs and caspases. Based on the structure of the IAP antagonist and recently reported thiadiazole derivatives, we designed and evaluated the biochemical properties of a series of phosphonic peptides bearing the N-Me-Ala-Val/Chg-Pro-OH motif (Chg: cyclohexylglycine). The ability of the obtained compounds to interact with the binding groove of the X-linked inhibitor of apoptosis protein baculovirus inhibitor of apoptosis protein repeat (XIAP BIR3) domain was examined by a fluorescence polarization assay, while their potential to induce autoubiquitination followed by proteasomal degradation of cellular IAP1 was examined using the MDA-MB-231 breast cancer cell line. The highest potency against BIR3 was observed among peptides containing C-terminal phosphonic phenylalanine analogs, which displayed nanomolar Ki values. Their antiproliferative potential as well as their proapoptotic action, manifested by an increase in caspase-3 activity, was examined using various cell lines.

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.

Toolbox of Fluorescent Probes for Parallel Imaging Reveals Uneven Location of Serine Proteases in Neutrophils

Neutrophils, the front line defenders against infection, express four serine proteases (NSPs) that play roles in the control of cell-signaling pathways and defense against pathogens and whose imbalance leads to pathological conditions. Dissecting the roles of individual NSPs in humans is problematic because neutrophils are end-stage cells with a short half-life and minimal ongoing protein synthesis. To gain insight into the regulation of NSP activity we have generated a small-molecule chemical toolbox consisting of activity-based probes with different fluorophore-detecting groups with minimal wavelength overlap and highly selective natural and unnatural amino acid recognition sequences. The key feature of these activity-based probes is the ability to use them for simultaneous observation and detection of all four individual NSPs by fluorescence microscopy, a feature never achieved in previous studies. Using these probes we demonstrate uneven distribution of NSPs in neutrophil azurophil granules, such that they seem to be mutually excluded from each other, suggesting the existence of unknown granule-targeting mechanisms.

Amidase activity of phosphonate analogue imprinted chymotrypsin mimics in shape-selective, substrate-specific and enantioselective amidolysis of l-phenylalanine-p-nitroanilides

Focusing on chymotrypsin mimics, highly crosslinked enzyme mimics are synthesized by molecular imprinting technique for the amidolysis of p-nitroanilide of phenylalanine, using phenyl-1-(N-benzyloxycarbonylamino)-2-(phenyl)ethyl phosphonate - the transition state analog of amidolysis - as the template, N-methacryloyl-l-histidine, N-methacryloyl-l-aspartic acid, and N-methacryloyl-l-serine as the functional monomers and EGDMA as the crosslinking agent. The amidase activity of the enzyme mimics follows pseudo first order kinetics. The transition state analog provides a tetrahedral geometry complementary to the transition state intermediate, which is responsible for the catalytic activity of the imprinted enzyme mimics. The enzyme mimics show stereospecificity and substrate selectivity in the amidolysis of phenylalanine p-nitroanilide. The proper orientation of the reactive functionalities in the super crosslinked macroporous polymer matrix for selective binding of the substrate through H-bonding is responsible for the high imprinting efficiency and substrate specificity of the imprinted polymer catalysts. Low cost, ease of preparation, high thermal stability, reusability and higher shelf life make the polymer catalysts better chymotrypsin mimics.