36992-14-0

Upstream product

• 84690-43-7 (1-Amino-2-phenyl-ethyl)-phosphonic acid dimethyl ester 
• 88024-05-9 C₃₈H₃₂NO₁₀P 
• 18108-22-0 1-amino-1-phenylmethylphosphonic acid 
• 6324-00-1 1-amino-2-phenylethanephosphonic acid 
• 135362-56-0 1-(N-Phenylacetylamino)-2-phenylethylphosphonic acid diisopropyl ester 
• 122-78-1 phenylacetaldehyde 
• 101-41-7 benzeneacetic acid methyl ester 
• 104513-36-2 1-(N-Phenylacetylamino)-2-phenylethylphosphonic acid 
• 150-30-1 Phenylalanine 
• 54582-05-7 N-phenylacetyl-3-phenyl-alanine 
• 145240-89-7 [2-Phenyl-1-((R)-4-phenyl-oxazolidin-3-yl)-ethyl]-phosphonic acid dimethyl ester 
• 145240-95-5 [1-((R)-2-Hydroxy-1-phenyl-ethylamino)-2-phenyl-ethyl]-phosphonic acid dimethyl ester 
• 100-39-0 benzyl bromide 

Downstream Products

• 90427-82-0 [(R)-1-Amino-2-(4-amino-phenyl)-ethyl]-phosphonic acid 
• 107072-62-8 ((R)-1-Benzyloxycarbonylamino-2-phenyl-ethyl)-phosphonic acid 
• 90427-81-9 [(R)-1-Amino-2-(4-nitro-phenyl)-ethyl]-phosphonic acid 
• 118867-00-8 (R)-(1-Amino-2-phenylethyl)phosphonsaeure-diethylester 

Relevant academic research and scientific papers

Biocatalyzed kinetic resolution of racemic mixtures of chiral α-aminophosphonic acids

Several fungal species namely: Aspergillus niger, Aspergillus parasiticus, Penicillium funiculosum, Trigonopsis variabilis and two different strains of Fusarium oxysporum were tested toward racemic mixtures of following phosphonic acids: 1-amino-2-methylp

A Methylidene Group in the Phosphonic Acid Analogue of Phenylalanine Reverses the Enantiopreference of Binding to Phenylalanine Ammonia-Lyases

Aromatic amino acid ammonia-lyases and aromatic amino acid 2,3-aminomutases contain the post-translationally formed prosthetic 3,5-dihydro-4-methylidene-5H-imidazol-5-one (MIO) group. MIO enzymes catalyze the stereoselective synthesis of α- or β-amino acid enantiomers, making these chemical processes environmentally friendly and affordable. Characterization of novel inhibitors enables structural understanding of enzyme mechanism and recognizes promising herbicide candidates as well. The present study found that both enantiomers of the aminophosphonic acid analogue of the natural substrate phenylalanine and a novel derivative bearing a methylidene at the β-position inhibited phenylalanine ammonia-lyases (PAL), representing MIO enzymes. X-ray methods unambiguously determined the absolute configuration of all tested enantiomers during their synthesis. Enzyme kinetic measurements revealed the enantiomer of the methylidene-substituted substrate analogue as being a mirror image relation to the natural l-phenylalanine as the strongest inhibitor. Isothermal titration calorimetry (ITC) confirmed the binding constants and provided a detailed analysis of the thermodynamic driving forces of ligand binding. Molecular docking suggested that binding of the (R)- and (S)-enantiomers is possible by a mirror image packing. (Figure presented.).

Penicillin G acylase-mediated kinetic resolution of racemic 1-(N-acylamino)alkylphosphonic and 1-(N-acylamino)alkylphosphinic acids and their esters

Extensive studies on the penicillin G acylase-mediated kinetic resolution of N-acylated 1-aminoalkylphosphonic and 1-aminoalkylphosphinic acids as well as their esters were carried out to recognise the relationships between the substrate structure, reacti

Enantioselective ester hydrolysis catalyzed by imprinted polymers. 2

Highly cross-linked network polymers prepared by molecular imprinting catalyzed enantioselectively the hydrolysis of N-tert-butoxycarbonyl phenylalanine-p-nitrophenyl ester (BOCPheONP). The templates were designed to allow incorporation of the key catalytic elements, found in the proteolytic enzyme chymotrypsin, into the polymer active sites. Three model systems were evaluated. These were constructed from a chiral phosphonate analogue of phenylalanine (series A, C) or L-phenylalanine (series B) attached by a labile ester linkage to an imidazole-containing vinyl monomer. Free radical copolymerization of the template with methacrylic acid (MAA) and ethylene glycol dimethacrylate (EDMA) gave a highly cross-linked network polymer. The templates could be liberated from the polymers by hydrolysis, giving catalytically active sites envisaged to contain an enantioselective binding site, a site complementary to a transition state like structure (series A, C), and a hydroxyl, imidazole, and carboxylic acid group at hydrogen bond distance. As predicted, the enantiomer of BOCPheONP complementary to the configuration of the template was preferentially hydrolyzed with D-selectivity for the series A polymers (kD/kL= 1.9) and L-selectivity for the series B polymers (kL/kD = 1.2). The maximum rate enhancement, when compared with a control polymer, prepared using a benzoyl-substituted imidazole monomer as template, was 2.5, and comparing with the imidazole monomer in solution, a maximum rate enhancement of 10 was observed. The catalytic activity was higher for polymers subjected to the nucleophilic treatment. This was explained by a higher site density and flexibility of the polymer matrix caused by this treatment. In a comparison of template rebinding to polymers imprinted with a template containing either a carboxylate (planar ground state structure) or a phosphonate (tetrahedral transition state like structure) functionality, it was observed that imprinted polymers are able to discriminate between a transition state like and a ground state structure for transesterification. However the influence of transition state stabilization on the observed rate enhancements remains obscure. Only at acidic pH's was catalysis observed, whereas at basic pH's the polymers inhibit the reaction. At a later stage, the catalytic activity of the polymers for nonactivated D- and L-phenylalanine ethyl esters was investigated. A rate enhancement of up to 3 was observed when compared to the blank. Most important, however, the polymers imprinted with a D template preferentially hydrolyzed the D-ethyl ester and exhibited saturation kinetics.

Synthesis of five enantiomerically pure haptens designed for in vitro evolution of antibodies with peptidase activity

A series of five haptens have been synthesized for use in in vitro selection experiments from combinatorial antibody libraries. Haptens were designed for the recruitment of serine and cysteine pretense reaction mechanisms for the cleavage of Phe-Ala and Phe-Phe (L,L) dipeptide analogues. For the selection of transition state stabilization, Phe(P)(O)Ala (7) and PheP(O)Phe (10) derivatives were synthesized using the Mitsunobu approach where Phe(P) represents the phosphonic acid analogue of phenylalanine and (O)Phe and (O)Ala represent (L)-β-phenyllactic and (L)-lactic acid, respectively. Optically pure peptidyl diazomethyl ketones 16 and 22 were synthesized for selection of the catalytic ensemble of cysteine proteases. An optically pure dipeptidyl boronic acid 26 was synthesized for the selection of the catalytic ensemble of serine proteases. A strategy for the evolution el catalytic antibodies using these haptens was developed which includes mechanism-based selections. Since mechanism based selections result in covalent trapping of species from libraries, diol and disulfide containing haptenic linkers were developed for the oxidative or reductive release of selected catalysts.

Design and synthesis of phosphinic acids that triply inhibit endothelin converting enzyme, angiotensin converting enzyme and neutral endopeptidase 24.11

We have synthesized a series of phosphinic acids as inhibitors of the metalloprotease endothelin converting enzyme (ECE). Potent ECE inhibitors 4g and 4o were identified. These compounds are members of a novel class of ECE inhibitors that are also potent inhibitors of angiotensin converting enzyme and neutral endopeptidase.

(1H-Benzotriazol-1-yloxy)tris(dimethylamino)phosphonium Hexafluorophosphate- and (1H-Benzotriazol-1-yloxy)tripyrrolidinophosphonium Hexafluorophosphate-Mediated Activation of Monophosphonate Esters: Synthesis of Mixed Phosphonate Diesters, the Reactivity of the Benzotriazolyl Phosphon...

A general method for synthesizing mixed phosphonate diesters from monoesters using (1H-benzotriazol-1-yloxy)tris(dimethylamino)phosphonium hexafluorophosphate or (1H-benzotriazol-1-yloxy)tripyrrolidinophosphonium hexafluorophosphate reagents is described.The reaction proceeded through a benzotriazolyl ester as shown by comparison with other reagents such as DCC, DCC/DMAP, DCC/1-hydroxybenzotriazole, bromotris(dimethylamino)phosphonium hexafluorophosphate, or O-(1H-benzotriazol-1-yl)-N,N,N',N'-tetramethyluronium hexafluorophosphate and by 31P NMR analysis.This benzotriazolyl phosphonic ester intermediate was more reactive toward alcohols than toward amines, contrary to its carboxylic analogue.

ASYMMETRIC SYNTHESIS OF 1-AMINOALKYLPHOSPHONIC ACIDS

Asymmetric synthesis of Phe and Tyr phosphonic analogous has been achieved by diastereoselective alkylation of chiral 1,2,3-oxazaphospholanes, the latter being readily obtained from (-) ephedrine and chloromethylphosphonic dichloride. Key words: (-)-Ephedrine; chloromethyl phosphonic dichloride; 1,3,2-oxazaphospholanes; optically active (S) and (R) 1-aminoalkylphosphonic acids.

A simple and general method for the asymmetric synthesis of α-aminophosphonic acids

A simple and general method for the asymmetric synthesis of α-aminophosphonic acids is described. A chiral phosphonate prepared in one step from R-(-)-phenylglycinol was alkylated with good diastereoselectivity using different electrophiles.

Preparation of optically active 1-aminoalkylphosphonic acids by stereoselective enzymatic hydrolysis of racemic N-acylated 1-aminoalkylphosphonic acids

N-Phenylacetylated derivatives of 1-aminoalkylphosphonic acids were synthesized and high enantioselectivity of their hydrolysis by penicillin acylase (EC 3.5.1.11) was demonstrated. Stereoselective enzymatic hydrolysis of racemic 1-(N-phenylacetylamino) alkylphosphonic acids was used for preparation of enantiomeric 1-aminoalkylphosphonic acids. The kinetic regularities of penicillin acylase catalyzed hydrolysis were established and the biocatalytic process was optimized to increase the optical purity and the yield of the optically active product.