51078-31-0

Basic information

• Product Name: BOC-LYS(Z)-PNA
• Synonyms: N-ALPHA-T-BUTYLOXYCARBONYL-N-EPSILON-BENZYLOXYCARBONYL-L-LYSINE 4-NITROANILID;N-ALPHA-TERT-BUTYLOXYCARBONYL-N-EPSILON-BENZYLOXYCARBONYL-L-LYSINE 4-NITROANILIDE;BOC-N-EPSILON-Z-L-LYSINE 4-NITROANILIDE;BOC-LYS(Z)-PNA;BOC-LYSINE(Z)-PNA;BOC-L-LYS(Z)-PNA;N-α-Boc-N-ε-Z-L-lysine 4-nitroanilide;N-a-Boc-N-e-Z-L-lysine4-nitroanilide
• CAS NO: 51078-31-0
• Molecular Formula: C₂₅H₃₂N₄O₇
• Molecular Weight: 500.54
• Product Categories: Boc-Amino Acids and Derivative;Boc-Amino acid series
• Mol File: 51078-31-0.mol

Chemical Properties

• Boiling Point: 739.1 °C at 760 mmHg
• Flash Point: 400.8 °C
• Appearance: /
• Density: 1.246
• Vapor Pressure: 1.04E-21mmHg at 25°C
• Refractive Index: 1.577
• Storage Temp.: -15°C
• CAS DataBase Reference: BOC-LYS(Z)-PNA(CAS DataBase Reference)
• NIST Chemistry Reference: BOC-LYS(Z)-PNA(51078-31-0)
• EPA Substance Registry System: BOC-LYS(Z)-PNA(51078-31-0)

Safety Data

• Hazardous Substances Data: 51078-31-0(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Industry:
BOC-LYS(Z)-PNA is used as a key intermediate for the synthesis of amino acid nitroanilides, which are important as chromogenic peptide substrates. These substrates are crucial for the development of assays to measure enzymatic activities, particularly for proteases and peptidases. The chromogenic nature of these substrates allows for easy detection and quantification of enzyme activity, making them valuable tools in research and drug discovery.
Used in Research Applications:
In the field of research, BOC-LYS(Z)-PNA is utilized for the preparation of peptide substrates that can be employed in studying enzyme kinetics, mechanism, and specificity. The ability to monitor enzyme activity through the release of p-nitroaniline upon substrate cleavage provides a convenient and sensitive method for assessing enzyme function and inhibition.
Used in Drug Discovery:
BOC-LYS(Z)-PNA plays a significant role in drug discovery, as the synthesized chromogenic peptide substrates can be used to screen for potential inhibitors of specific enzymes. This is particularly important in the development of therapeutic agents targeting proteases and peptidases implicated in various diseases, including cancer, inflammation, and infectious diseases.

InChI:InChI=1/C25H32N4O7/c1-25(2,3)36-24(32)28-21(22(30)27-19-12-14-20(15-13-19)29(33)34)11-7-8-16-26-23(31)35-17-18-9-5-4-6-10-18/h4-6,9-10,12-15,21H,7-8,11,16-17H2,1-3H3,(H,26,31)(H,27,30)(H,28,32)/t21-/m0/s1

Upstream product

• 2389-45-9 Boc-Lys(Z)-OH 
• 100-01-6 4-nitro-aniline 
• 62-23-7 4-nitro-benzoic acid 
• 134393-23-0 N,N'-bis(4-nitrophenyl)phospheneimidous amide 

Downstream Products

• 62354-37-4 N-Z-D-valyl-leucyl-N^ε-Z-lysine p-nitroanilide 
• 128992-45-0 D-valyl-leucyl-lysine p-nitroanilide dihydrobromide 
• 138865-32-4 [(S)-5-{[4-(Benzyloxycarbonylamino-methyl)-cyclohexanecarbonyl]-amino}-5-(4-nitro-phenylcarbamoyl)-pentyl]-carbamic acid benzyl ester 
• 75736-21-9 HCl*H-Lys(Z)-pNA 
• 61876-77-5 H-Lyz(Z)-pNA 
• 85705-14-2 Suc-Tyr-Leu-Lys-pNA acetate 
• 85697-98-9 [(S)-5-{(S)-2-[(S)-2-Amino-3-(4-hydroxy-phenyl)-propionylamino]-4-methyl-pentanoylamino}-5-(4-nitro-phenylcarbamoyl)-pentyl]-carbamic acid benzyl ester; hydrochloride 
• 85705-12-0 Suc-Tyr-Leu-Lys(Z)-pNA 
• 85697-88-7 Boc-Tyr-Leu-Lys(Z)-pNA 
• 85698-10-8 H-Leu-Lys(Z)-pNA*HCl 
• 51078-32-1 Boc-Leu-Lys(Z)-pNA 

Relevant articles and documents

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.