5679-61-8

Upstream product

• 106-48-9 4-chloro-phenol 
• 7719-12-2 phosphorus trichloride 

Downstream Products

• 94578-41-3 N--carbamidsaeuremethylester 
• 860180-81-0 di-(4-chlorophenyl) phosphite 
• 13388-88-0 4-chlorophenyl phosphate 
• 79227-87-5 Phosphorsaeure-p-chlorphenylester Cyclohexylammonium salz 
• 52602-94-5 4'-Nitrobenzyl 7-amino-3-methyl-3-cephem-4-carboxylate hydrochloride 
• 72868-04-3 (CO)3NiP(OC₆H₄Cl-p)3 
• 198983-79-8 cis-[PtClMe(tris-(4-chlorophenyl) phosphite)2] 
• 1244955-95-0 C₂₆H₂₇Cl₂O₄P 
• 1244955-96-1 C₂₆H₂₇Cl₂O₄P 
• 161290-53-5 C₂₄H₂₄Cl₂NO₅P 
• 161290-57-9 BrH*C₁₆H₁₈Cl₂NO₃P 
• 1275615-41-2 1-isocyano-2-methylpropanephosphonic acid di(4-chlorophenyl) ester 

Relevant academic research and scientific papers

New selective peptidyl di(chlorophenyl) phosphonate esters for visualizing and blocking neutrophil proteinase 3 in human diseases

The function of neutrophil protease 3 (PR3) is poorly under-stood despite of its role in autoimmune vasculitides and its possible involvement in cell apoptosis. This makes it different from its structural homologue neutrophil elastase (HNE). Endogenous inhibitors of human neutrophil serine proteases preferentially inhibit HNE and to a lesser extent, PR3. We constructed a single-residue mutant PR3 (I217R) to investigate the S4 subsite preferences of PR3 and HNE and used the best peptide substrate sequences to develop selective phosphonate inhibitors with the structure Ac-peptidylP(0-C6H4-4-Cl)2. The combination of a prolyl residue at P4 and an aspartyl residue at P2 was totally selective for PR3. We then synthesized N-terminally biotinylated peptidyl phosphonates to identify the PR3 in complex biological samples. These inhibitors resisted proteolytic degradation and rapidly inactivated PR3 in biological fluids such as inflammatory lung secretions and the urine of patients with bladder cancer. One of these inhibitors revealed intracellular PR3 in permeabilized neutrophils and on the surface of activated cells. They hardly inhibited PR3 bound to the surface of stimulated neutrophils despite their low molecular mass, suggesting that the conformation and reactivity of membrane-bound PR3 is altered. This finding is relevant for autoantibody binding and the subsequent activation of neutrophils in granulomatosis with polyangiitis (formerly Wegener disease). These are the first inhibitors that can be used as probes to monitor, detect, and control PR3 activity in a variety of inflammatory diseases.

Exploiting the S4-S5 Specificity of Human Neutrophil Proteinase 3 to Improve the Potency of Peptidyl Di(chlorophenyl)-phosphonate Ester Inhibitors: A Kinetic and Molecular Modeling Analysis

The neutrophilic serine protease proteinase 3 (PR3) is involved in inflammation and immune response and thus appears as a therapeutic target for a variety of infectious and inflammatory diseases. Here we combined kinetic and molecular docking studies to i

Phosphonic Analogs of Alanine as Acylpeptide Hydrolase Inhibitors

Acylpeptide hydrolase is a serine protease, which, together with prolyl oligopeptidase, dipeptidyl peptidase IV and oligopeptidase B, belongs to the prolyl oligopeptidase family. Its primary function is associated with the removal of N-acetylated amino acid residues from proteins and peptides. Although the N-acylation occurs in 50–90 % of eukaryotic proteins, the precise functions of this modification remains unclear. Recent findings have indicated that acylpeptide hydrolase participates in various events including oxidized proteins degradation, amyloid β-peptide cleavage, and response to DNA damage. Considering the protein degradation cycle cross-talk between acylpeptide hydrolase and proteasome, inhibition of the first enzyme resulted in down-regulation of the ubiquitin-proteasome system and induction of cancer cell apoptosis. Acylpeptide hydrolase has been proposed as an interesting target for the development of new potential anticancer agents. Here, we present the synthesis of simple derivatives of (1-aminoethyl)phosphonic acid diaryl esters, phosphonic analogs of alanine diversified at the N-terminus and ester rings, as inhibitors of acylpeptide hydrolase and discuss the ability of the title compounds to induce apoptosis of U937 and MV-4-11 tumor cell lines.

A fluorinated phosphite traps alkoxy radicals photogenerated at the air/solid interface of a nanoparticle

With interests in alkoxy radical formation on natural and artificial surfaces, a physical-organic study was carried out with a Hammett series of triaryl phosphites (p-MeO, H, p-F, and p-Cl) to trap adsorbed alkoxy radicals on silica nanoparticles. A mecha

Electronic effects in mixed N-heterocyclic carbene/phosphite indenylidene ruthenium metathesis catalysts

Five new complexes [RuCl2(SIMes)(Ind)(O-pXC5H4)] bearing different para-substituted triphenylphosphites (X = H, OCH3, CF3, Cl, SF5 and CN) were synthesised and used to study the effect of t

Phosphonate prodrug of adenine derivative and medical application of phosphonate prodrug

The invention relates to a phosphonate prodrug of an adenine derivative and medical application of the phosphonate prodrug. Specifically, the invention relates to a compound shown in a general formula (I) or an optical isomer, or a pharmaceutical salt, or

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.

Human neutrophil elastase phosphonic inhibitors with improved potency of action

Herein, we present the synthesis and the measurement of the inhibitory activity of novel peptidyl derivatives of α-aminoalkylphosphonate diaryl esters as human neutrophil elastase inhibitors. Their selectivity against other serine proteases, including porcine pancreatic elastase, chymotrypsin, and trypsin, was also demonstrated. We also describe the preparation of single peptide diastereomers. The most active and selective compound developed possessed a kinact/KI of 2353000 M-1 s -1, which is the most potent irreversible peptidyl inhibitor of human neutrophil elastase reported to date. The peptidyl inhibitors were demonstrated to be stable in PBS buffer and human plasma, as were their complexes with HNE.

Phosphonic pseudopeptides as human neutrophil elastase inhibitors - A combinatorial approach

Here we present a simple and rapid method for the construction of phosphonic peptide mimetic inhibitor libraries - products of Ugi and Passerini multicomponent condensations - leading to the selection of new biologically active phosphonic pseudopeptides.

Simple phosphonic inhibitors of human neutrophil elastase

Herein, we describe the synthesis and resulting activity of a complex series of α-aminophosphonate diaryl esters as irreversible human neutrophil elastase inhibitors and their selectivity preference for human neutrophil elastase over several other serine proteases such as porcine pancreatic elastase, trypsin, and chymotrypsin. We synthesized and examined the inhibitory potency of several new simple Cbz-protected α- aminoalkylphosphonate diaryl esters that yielded several new HNE inhibitors, where one of the obtained compounds Cbz-ValP(OC6H 4-4-COOMe)2 displayed an apparent second-order inhibition value at 33,015 M-1 s-1.