17663-35-3

Upstream product

• 2578-84-9 N-benzyloxycarbonyl-L-phenylalanine p-nitrophenyl ester 
• 55895-89-1 D,L-phenylalanine p-nitrophenyl ester 
• 75531-06-5 2-Decanoylamino-3-phenyl-propionic acid 4-nitro-phenyl ester 
• 14009-94-0 p-nitrophenyl N-acetyl-L-phenylalaninate 
• 2578-84-9 p-nitrophenyl N-(benzyloxycarbonyl)-L-phenylalaninate 
• 75531-06-5 2-Decanoylamino-3-phenyl-propionic acid 4-nitro-phenyl ester 
• 14009-95-1 p-nitrophenyl N-acetyl-D-phenylalaninate 
• 2578-85-0 p-nitrophenyl N-(benzyloxycarbonyl)-D-phenylalaninate 
• 100-02-7 4-nitro-phenol 
• 7535-56-0 N-t-butoxycarbonyl-L-phenylalanine 4-nitrophenyl ester 
• 38806-34-7 p-Nitrophenyl 
• 13734-34-4 N-tert-butoxycarbonyl-L-phenylalanine 
• 75531-07-6 p-nitrophenyl n-dodecanoyl-D(L)-phenylalaninate 

Downstream Products

• 96980-05-1 Tritylsulfenyl-Phe-ONP 
• 146056-44-2 (S)-2-Butyrylamino-3-phenyl-propionic acid 4-nitro-phenyl ester 
• 96675-19-3 Tritylsulfenyl-Phe-Gly-OEt 
• 75531-12-3 N-dodecanoyl-D-phenylalanine 4-nitrophenylester 
• 75531-11-2 N-dodecanoyl-L-phenylalanine 4-nitrophenylester 
• 100-02-7 4-nitro-phenol 
• 63-91-2 L-phenylalanine 
• 673-06-3 D-β-Phenyl-α-alanine 
• 130306-87-5 N-((S)-1-{3-[4-(3-Amino-propylamino)-butylamino]-propylcarbamoyl}-2-phenyl-ethyl)-butyramide 
• 118404-30-1 (S)-2-[(S)-2-(2-Benzyloxycarbonylamino-acetylamino)-propionylamino]-3-phenyl-thiopropionic acid S-[2-(2-{(2S,3S)-3-[2-(2-mercapto-ethoxy)-ethoxymethyl]-1,4,7,10,13,16-hexaoxa-cyclooctadec-2-ylmethoxy}-ethoxy)-ethyl] ester 
• 15112-71-7 N-benzyloxycarbonylglycyl-L-alanyl-L-phenylalanine methyl ester 
• 29588-02-1 NPS-Phe-ONP 
• 96980-02-8 Trityl-Phe-ONP 

Relevant academic research and scientific papers

High Stereoselectivity in the Deacylation of p-Nitrophenyl N-Acylphenylalanates by Bilayer Vesicular Systems which include Dipeptide-type Nucleophiles

The deacylation of p-nitrophenyl N-acylphenylalanates with bilayer vesicular systems comprising dipeptide-type nucleophiles and a cationic double chain surfactant resulted in high stereoselectivity (kLcat/kDcat = 29.6 at 25 deg C and 83.6 at 10 deg C) for the deacylation of p-nitrophenyl N-dodecanoylphenylalanate by the catalytic system of N-(N-benzyloxycarbonyl-L-leucyl)-L-histidine and N,N-didodecyl-N,N-dimethylammonium bromide.

Enantioselective Deacylation of Long Chain p-Nitrophenyl N-Acylphenylalanates by N-(N-Dodecanoyl-L-histidyl)-L-leucine and a Cationic Chiral Surfactant

Enhanced enantioselectivity (kcatL/kcatD 5.5-5.7) was observed in the deacylation of Hn-1CONHCH(CH2Ph)CO2C6H4NO2-p possessing long acyl chains (n 10-16) by comicelles of N-(N-dodecanoyl-L-histidyl)-L-leucine and (R)-(+)-N-α-methylbenzyl-NN-dimethyloctadecylammonium bromide.

Designed Negative Feedback from Transiently Formed Catalytic Nanostructures

Highly dynamic and complex systems of microtubules undergo a substrate-induced change of conformation that leads to polymerization. Owing to the augmented catalytic potential at the polymerized state, rapid hydrolysis of the substrate is observed, leading to catastrophe, thus realizing the out-of-equilibrium state. A simple synthetic mimic of these dynamic natural systems is presented, where similar substrate induced conformational change is observed and a transient helical morphology is accessed. Further, augmented catalytic potential of these helical nanostructures leads to rapid hydrolysis of the substrate providing negative feedback on the stability of the nanostructures and realization of an out-of-equilibrium state. This simple system, made from amino acid functionalized lipids, demonstrates a substrate-induced self-assembled state, where the fuel-to-waste conversion leads to the temporal presence of helical nanostructures.

Capillary electrophoretic separation of enantiomers of amino acids and amino acid derivatives using crown ether and cyclodextrin

The capillary zone electrophoresis using (+)-18-crown-6-tetracarbonic acid as a chiral selector was a suitable method for the enantiomeric separation of racemates of amino acids and of some amino acid derivatives (esters, dipeptides). The influence of the chemical structure of the compounds on the separation was investigated. After optimization of the separation conditions, baseline separations were obtained for most racemates. The addition of acetonitrile and TBAB yielded an improvement of the separation. Improved selectivity was further observed by the application of a cyclodextrin, HP-β-CD, in combination with the crown ether.

Kinetic study on conformational effect in hydrolysis of p-nitroanilides catalyzed by α-chymotrypsin

Effects of medium viscosity on kinetics for the hydrolysis of p-nitroanilides of certain amino acid derivatives catalyzed by α-chymotrypsin have been investigated. Observed data indicate that the overall rate constant, kcat, is hardly affected by the medium viscosity in all the substrates employed and equals the rate constant at the acylation step, k2, in the measured range of viscosity. By comparison with the data on p-nitrophenyl ester substrates reported previously, it is concluded that the formation of the tetrahedral intermediate in the course of the acylation of the enzyme is influenced by conformational change of the enzyme, whereas the breakdown of the intermediate is almost free from conformational effects.

Mechanism of Enantioselective Ester Cleavage by Histidine-Containing Dipeptides at a Micellar Interface

Chiral p-nitrophenyl esters derived from the amino acid phenylalanine are cleaved by histidine-containing dipeptides at a micellar interface.High enantioselectivities (up to kL/kD = 30.4 at 0 deg C) are observed.Both the substrates and the catalysts contain an alternating sequence of hydrophobic and hydrophilic groups.Due to the need for hydration of the hydrophilic groups, the hydrophobic groups cannot dissolve completely into the micellar hydrocarbon phase.The kinetic data suggest that the micellar interface is capable of discriminating between transition states that have different hydrophilic and hydrophobic properties.One of the diastereomeric transition states is characterized by a hydrogen bond between the amide CO group of the ester and an NH group of the histidine-containing dipeptide.Upon formation of this hydrogen bond these polar CO and NH groups lose their hydrophilicity which allows the transfer of the adjacent apolar groups to the micellar hydrocarbon phase.The other diastereomeric transition state cannot form this hydrogen bond and the hydrophobic groups remain hydrated.Consequently, the latter transition state is of higher energy.The kinetic data reveal that it is important to prevent steric hinderance between the reactants in order to allow the unhindered formation of the hydrogen bond.