2578-85-0

Usage

Uses

Used in Biochemical Research:
Z-D-PHE-ONP is used as a substrate for enzymatic reactions to study the activity and kinetics of proteases. Its unique property of undergoing a colorimetric change upon cleavage by proteases makes it a reliable tool for monitoring enzyme activity in various biochemical assays.
Used in Pharmaceutical Research:
In the pharmaceutical industry, Z-D-PHE-ONP is employed as a component in the development and testing of potential therapeutic agents. Its application extends to the study and treatment of various diseases and conditions, including cancer and inflammatory disorders, where protease activity is a significant factor.
Used in Diagnostics:
Z-D-PHE-ONP is used as a diagnostic tool for the detection and measurement of protease activity, particularly in the study of blood coagulation and fibrinolysis. Its colorimetric response to protease action aids in the assessment of related physiological processes and can contribute to the diagnosis of related conditions.
Used in Enzyme Inhibitor Screening:
Z-D-PHE-ONP is utilized as a screening agent for the identification of potential enzyme inhibitors. By observing the effect of different compounds on the protease-induced colorimetric change, researchers can evaluate the inhibitory potential of new drug candidates against specific proteases.

Upstream product

• 100-02-7 4-nitro-phenol 
• 2448-45-5 Cbz-D-Phe 

Downstream Products

• 83575-47-7 benzyloxycarbonyl-D-phenylalanyl-L-prolyl-L-citrulline p-nitroanilide 
• 100-02-7 4-nitro-phenol 
• 2448-45-5 Cbz-D-Phe 
• 14609-74-6 p-nitrophenolate 
• 1238-09-1 N^α-phenylalanyl-arginine 
• 127292-75-5 AsnDPheTrpAlaValGlyHisLeuMetNH₂ 
• 127292-67-5 (S)-2-{(S)-2-[(S)-2-[(R)-2-((S)-2-tert-Butoxycarbonylamino-3-carbamoyl-propionylamino)-3-phenyl-propionylamino]-3-(1H-indol-3-yl)-propionylamino]-propionylamino}-3-methyl-butyric acid 
• 127317-00-4 (S)-2-[(R)-2-((S)-2-tert-Butoxycarbonylamino-3-carbamoyl-propionylamino)-3-phenyl-propionylamino]-3-(1H-indol-3-yl)-propionic acid 
• 127292-68-6 C₅₆H₈₀N₁₄O₁₂S 
• 75531-12-3 N-dodecanoyl-D-phenylalanine 4-nitrophenylester 
• 17663-35-3 p-Nitrophenyl-D-phenylalaninate 
• 2448-45-5 N-(Benzyloxycarbonyl)-D-phenylalanine 
• 17460-79-6 N-Cbz-D-Phe-L-Trp-OH 
• 2682-76-0 Boc-Ala-D-Phe-Ile-Gly-OEt 

Relevant academic research and scientific papers

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.

Hybrid Liposomes Coupled to Steric Control with High Enantioselectivity

With respect to the hydrolysis of enantiomeric substrates (p-nitrophenyl N-dodecanoyl-D(L)-phenylalaninate; C12-D(L)-Phe-PNP) by the tripeptide catalyst (N-(benzyloxycarbonyl)-L-phenylalanyl-L-histidyl-L-leucine; Z-PheHisLeu), a remarkably high enantioselectivity (kLa/obsd/kDa/obsd = 28) along with marked rate-enhancement of the hydrolytic cleavage of C12-D(L)-Phe-PNP was obtained with specific coaggregates of 32 mol percent L-α-dipalmitoylphosphatidylcholine (DPPC) and 68 mol percent α--ω-hydroxypoly(oxy-1,2-ethanediyl) (TritonX-100).The enantioselectivity was maximized at the phase transition temperature (Tc) in the 65 mol percent DPPC/35 mol percent TritonX-100 and 32 mol percent DPPC/68 mol percent TritonX-100 coaggregate systems.The hydrophobicity and fluidity of the coaggregates can apparently be changed around Tc on the basis of isokinetic temperature and fluorescence parameter studies.

Cyclic dipeptide enantiomers

The invention provides novel cyclic dipeptide enantiomers comprising (R)-histidine or a derivative thereof as one of the amino acid residues. These compounds are useful a catalysts for production of (S) -α--cyanomethyl alcohols from aldehydes.