2360-97-6

Basic information

• Product Name: H-PHE-PNA HCL
• Synonyms: H-PHE-PNA HCL;H-L-PHE-PNA;L-PHENYLALANINE-P-NITROANILIDE;L-PHENYLALANINE 4-NITROANILIDE;L-PHENYLALNINE-P-NITROANILIDE;L-Phenylalanine 4-nitroanilide45 / 5g;H-L-Phe-pNA*HCl;L-Phenylalnine-p-nitroanilide hydrochloride
• CAS NO: 2360-97-6
• Molecular Formula: C₁₅H₁₅N₃O₃
• Molecular Weight: 321.76
• Mol File: 2360-97-6.mol
• Article Data: 10

Chemical Properties

• Boiling Point: 543.036 °C at 760 mmHg
• Flash Point: 282.218 °C
• Appearance: /
• Density: 1.323 g/cm³
• Storage Temp.: -15°C
• Solubility: Chloroform (Slightly), Dichloromethane (Slightly), Methanol (Slightly, Sonicated
• CAS DataBase Reference: H-PHE-PNA HCL(CAS DataBase Reference)
• NIST Chemistry Reference: H-PHE-PNA HCL(2360-97-6)
• EPA Substance Registry System: H-PHE-PNA HCL(2360-97-6)

Safety Data

• Safety Statements: S22:Do not inhale dust.; S24/25:Avoid contact with skin and eyes.
• Hazardous Substances Data: 2360-97-6(Hazardous Substances Data)

Usage

Description

H-PHE-PNA HCL, also known as L-Phenylalanine 4-Nitroanilide, is a light yellow powder that serves as a substrate for various enzymatic reactions. It is commonly used in the study and analysis of aminopeptidase M (microsomal alanyl aminopeptidase) and other cytosolic leucyl aminopeptidases.

Uses

Used in Pharmaceutical Industry:
H-PHE-PNA HCL is used as a substrate for aminopeptidase M (microsomal alanyl aminopeptidase) for the study and analysis of enzyme activity and function. This application aids in understanding the role of these enzymes in various biological processes and their potential as therapeutic targets.
Used in Research and Development:
H-PHE-PNA HCL is used as a substrate in the study of a novel cytosolic leucyl aminopeptidase. This application helps researchers investigate the properties and functions of these enzymes, which can contribute to the development of new drugs and therapies.
Used in Diagnostics:
H-PHE-PNA HCL can be employed in the development of diagnostic tools and assays to measure the activity of aminopeptidases. This can be useful in the detection and monitoring of various diseases and conditions related to enzyme dysfunction.
Used in Biochemical Education:
As a substrate for enzymatic reactions, H-PHE-PNA HCL can be utilized in educational settings to teach students about enzyme kinetics, mechanisms, and the role of enzymes in biological systems.

Upstream product

• 14235-15-5 benzyl (S)-(1-((4-nitrophenyl)amino)-1-oxo-3-phenylpropan-2-yl)carbamate 
• 97885-48-8 N-(1,1-dimethylethoxycarbonyl)-L-phenylalanine N-(4-nitrophenyl)amide 
• 100-01-6 4-nitro-aniline 
• 2448-45-5 Cbz-D-Phe 
• 13734-34-4 N-tert-butoxycarbonyl-L-phenylalanine 
• 5241-58-7 L-Phenylalanine amide 
• 586-78-7 para-nitrophenyl bromide 
• 100-00-5 4-chlorobenzonitrile 
• 61043-41-2 H-Ala-Ala-Phe-p-nirtoanilide 

Downstream Products

• 63276-82-4 benzyloxycarbonylglycyl-glycyl-phenylalanine p-nitroanilide 
• 63-91-2 L-phenylalanine 
• 100-01-6 4-nitro-aniline 
• 21027-71-4 {[(S)-1-(4-Nitro-phenylcarbamoyl)-2-phenyl-ethylcarbamoyl]-methyl}-carbamic acid benzyl ester 
• 85733-98-8 pyroglutamyl-L-phenylalanine p-nitroanilide 
• 186023-46-1 ((S)-2-Methyl-1-{(S)-4-[(S)-1-(4-nitro-phenylcarbamoyl)-2-phenyl-ethylcarbamoyl]-oxazolidine-3-carbonyl}-propyl)-carbamic acid 9H-fluoren-9-ylmethyl ester 
• 2440-62-2 N-(3-carboxypropionyl)-L-phenylalanine p-nitroanilide 
• 70968-17-1 Boc-Leu-Phe-pNA 

Relevant articles and documents

A molecular probe with both chromogenic and fluorescent units for detecting serine proteases

A molecular probe with L-phenylalanine p-nitroanilide and L-lysin 4-methylcoumaryl-7-amide, in which these amino acid derivatives are connected through a succinic-acid spacer, was prepared. Trypsin and papain were detected by blue-fluorescence emission of generated 7-amino-4-methylcoumarin (AMC). α-Chymotrypsin and nattokinase were detected from both the blue-fluorescence emission of AMC and the UV absorbance of p-nitroaniline. In addition, different time courses of p-nitroaniline and AMC were observed between the reaction of P1 with α-chymotrypsin and that with nattokinase. In the case of nattokinase, both the fluorescence emission and UV absorbance slowly increased. In contrast, the increasing UV absorbance was saturated at the early stage of the reaction of the present probe with chymotrypsin, whereas the fluorescence emission continuously increased in the following stages.

Synthesis of chiral amino acid anilides by ligand-free copper-catalyzed selective N-arylation of amino acid amides

An atom-economic, practical and cost-effective protocol for synthesis of chiral amino acid anilides via ligand-free copper-catalyzed selective C-N cross coupling of chiral amino acid amides and aryl halides, hetereoaryl halides and a vinyl bromide has been developed. No racemization occurred during the C-N coupling. A plausible mechanism is proposed. Copyright

Local and tunable n→π* interactions regulate amide isomerism in the peptoid backbone

We report that n→π* interactions are operative in peptoids and play a major role in controlling amide isomerism. These interactions can be tuned using α-chiral amide side chains known to promote peptoid folding. To our knowledge, this is the first report of n→π* interactions between amides in non-prolyl systems. Furthermore, we have characterized an n→π* interaction between backbone carbonyls and side chain aromatic rings that can dramatically stabilize the cis-amides required for peptoid helix formation. The tunability of both types of n→π* interactions in peptoids has significant implications for peptoid folding and could be exploited for the design of new peptoid architectures. Copyright