19647-71-3

Usage

Chemical Properties

White crystalline powder

Uses

Z-L-Phe-pNA is a chromogenic substrate.

Upstream product

• 1161-13-3 N-Cbz-L-Phe 
• 100-01-6 4-nitro-aniline 
• 2448-45-5 Cbz-D-Phe 
• 134393-23-0 N,N'-bis(4-nitrophenyl)phospheneimidous amide 

Downstream Products

• 2360-97-6 L-phenylalanine-p-nitroanilide 
• 78106-64-6 H-Phe-pNA*HBr 
• 1161-13-3 N-Cbz-L-Phe 
• 100-01-6 4-nitro-aniline 
• 85704-49-0 Boc-Tyr-Leu-Phe-pNA 
• 82155-60-0 Suc-Tyr-Leu-Phe-pNA 
• 85697-94-5 H-Tyr-Leu-Phe-pNA*HCl 
• 70968-17-1 Boc-Leu-Phe-pNA 
• 75651-89-7 H-Leu-Phe-pNA*HCl 
• 102292-77-3 Boc-L-Tyr-D-Leu-L-Phe-pNA 
• 99251-92-0 Suc-L-Tyr-D-Leu-L-Phe-pNA 
• 99242-15-6 H-D-Leu-L-Phe-pNA 
• 102292-75-1 Boc-D-Leu-L-Phe-pNA 
• 1361510-35-1 (S)-benzyl 1-(4-nitrophenylamino)-3-phenyl-1-selenoxopropan-2-ylcarbamate 

Relevant academic research and scientific papers

Ligand-Accelerated Palladium(II)-Catalyzed Enantioselective Amination of C(sp2)-H Bonds

The first example of the Pd(II)-catalyzed enantioselective amination of aryl C-H bonds is reported. The key to the successful realization of this asymmetric catalytic transformation was the identification of mono-N-protected α-amino-O-methylhydroxamic acid (MPAHA) ligands, which promote reactivity under mild conditions and control enantioselectivity. The counteranions in the solvent medium, hexafluoroacetylacetate and acetate, were also found to play key roles in stereocontrol and reactivity enhancement.

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.

Amidase activity of phosphonate TSA-built polymer catalysts derived from organic monomers in the amidolysis of amino acid p-nitroanilides

Highly crosslinked transition state analogue imprinted macromatric polymer catalysts having imidazole, carboxyl and hydroxyl functional groups in the catalytic sites were synthesized as chymotrypsin mimics using achiral organic monomers 4-vinylimidazole, methacrylic acid, allyl alcohol and phenyl-1-(N-benzyloxycarbonylamino)-2-(phenyl)ethyl phosphonate (transition state analogue of ester and amide hydrolytic reactions) as the template. The catalytic properties of the enzyme mimics were investigated in the amidolytic reactions of L-amino acid p-nitroanilides and correlated to the amidase activities of the catalysts derived from chiral methacryloyl-L-amino acid monomers methacryloyl-L-histidine, methacryloyl-L-aspartic acid and methacryloyl-L-serine. A two-fold enhancement in rate acceleration, substrate specificity, substrate shape-selectivity and stereoselectivity was observed for polymers made up of flexible amino acid monomers compared to the copolymers of organic monomers. The pre-polymerization complex of TSA with methacryloyl-L-amino acid monomers fabricates specific 3D-memory cavity preferentially of L-enantiomer of the TSA in the polymer matrix while the achiral organic monomers designs both L- and D- cavities The effect of crosslink density on the catalytic efficiencies of the polymer catalysts was also investigated. Replacement of allyl alcohol by vinylpyridine afforded catalyst with better enzymatic activity.

Synthesis of selenoxo peptides and oligoselenoxo peptides employing LiAlHSeH

Synthesis of selenoxo peptides by the treatment of Nα- protected peptide esters with a combination of PCl5 and LiAlHSeH is delineated. The method is simple, high-yielding, and free from racemization. Thus obtained selenoxo peptides are used as units for N-terminal chain extension through Nα-deprotection/coupling to yield peptide-selenoxo peptide hybrids. Multiple selenation is demonstrated by conversion of two peptide bonds of tripeptides into selenoxo peptide bonds. Amino acid derived arylamides are also converted into aryl selenoamides. C6H 5-CSeNH-Val-OMe 8f is obtained as single crystal, and its structure was determined through X-ray diffraction study.

A convenient synthesis of amino acid arylamides utilizing methanesulfonyl chloride and N-methylimidazole

N-Cbz-protected amino acids reacted with various aryl-amines in the presence of methanesulfonyl chloride and N-methylimidazole in dichloromethane to give the corresponding arylamides in high yields. No obvious racemization was observed under the mild conditions. Georg Thieme Verlag Stuttgart - New York.

Enzymatic synthesis of C-terminal arylamides of amino acids and peptides

(Chemical Equation Presented) A mild and cost-efficient chemo-enzymatic method for the synthesis of C-terminal arylamides of amino acid and peptides is described. Using the industrial serine protease Alcalase under near-anhydrous conditions, C-terminal arylamides of N-Cbz-protected amino acids and peptides could be obtained from the corresponding C-terminal carboxylic acids, methyl (Me) or benzyl (Bn) esters, in high chemical and enantio- and diastereomeric purities. Yields ranged between 50% and 95% depending on the size of the aryl substituents and the presence of electron-withdrawing substituents. Complete α-C-terminal selectivity could be obtained even in the presence of various unprotected side-chain functionalities such as β/γ-carboxyl, hydroxyl, and guanidino groups. In addition, the use of the cysteine protease papain and the lipase Cal-B gave anilides in high yields. The chemo-enzymatic synthesis of arylamides proved to be completely free of racemization, in contrast to the state-of-the-art chemical methods.

Fairly marked enantioselectivity for the hydrolysis of amino acid esters by chemically modified enzymes

The hydrolysis (deacylation) of enantiomeric substrates by the chemically modified enzymes decanoyl-α-chymotrypsin and decanoyl-trypsin was studied. Reaction activity for decanoyl-α-chymotrypsin was lower than that for the native enzyme, although intriguingly the enantioselectivity was markedly enhanced as compared with the native enzyme. In particular, the apparently complete enantioselective catalysis was attained for the hydrolytic cleavage of p-nitrophenyl N-dodecanoyl- D(L)-phenylalaninates. The enhancement of enantioselectivity, however, was not observed for decanoyl-trypsin. These results suggest that the chemically modified α-chymotrypsin by addition of hydrophobic groups has promoted enantioselectivity for the hydrolysis of hydrophobic esters.

A convenient synthesis of amino acid p-nitroanilides; synthons in the synthesis of protease substrates

A method is described for the synthesis of N(α)-protected bi- and trifunctional amino acid p-nitroanilides. The reaction uses phosphorus oxychloride as the condensing agent. The synthesis is simple, rapid, free of racemization and affords yields between 70-90%. The synthesis can be performed not only with amino acid derivatives of the urethane type including acid-labile (Z, Boc) and base-labile (Fmoc, Msc) N(α)-protective functions or allyl-derived protections, but also with N(α)-trityl amino acids, albeit in lower yield. The reaction runs in pyridine and its mechanism implies carboxyl activation by formation of a mixed anhydride with phosphorodichloridic acid (HOPOCl2).

Reinvestigation of the Phosphazo Method and Synthesis of N-(t-Butoxycarbonyl)-L-arginine p-Nitroanilide and a Chromogenic Enzyme Substrate for the Factor Xa

Reaction conditions for the phosphazo method were reinvestigated in order to apply this method to the synthesis of p-nitroanilide(pNA)s of t-butoxycarbonyl(Boc)- and benzyloxycarbonyl(Z)-amino acids.