133410-92-1

Basic information

• Product Name: H-D-ARG-PHE-OH
• Synonyms: H-D-ARG-PHE-OH
• CAS NO: 133410-92-1
• Molecular Formula: C15H23N5O3
• Molecular Weight: 321.37
• Mol File: 133410-92-1.mol
• Article Data: 5

Chemical Properties

• Appearance: /
• Storage Temp.: -15°C
• CAS DataBase Reference: H-D-ARG-PHE-OH(CAS DataBase Reference)
• NIST Chemistry Reference: H-D-ARG-PHE-OH(133410-92-1)
• EPA Substance Registry System: H-D-ARG-PHE-OH(133410-92-1)

Safety Data

• Hazardous Substances Data: 133410-92-1(Hazardous Substances Data)

Usage

General Description

H-D-ARG-PHE-OH, also known as N-Acetyl-L-phenylalanine, is a synthetic chemical compound consisting of the amino acids arginine and phenylalanine. It is a dipeptide, meaning it is composed of two amino acids linked together through a peptide bond. H-D-ARG-PHE-OH is commonly used as a substrate for enzymes involved in the production and degradation of amino acids, and it is also utilized in biochemical research to study the mechanisms of peptide bond formation and hydrolysis. Additionally, H-D-ARG-PHE-OH has potential applications in the pharmaceutical industry for the development of novel therapeutic agents. Overall, this compound has diverse uses in scientific research and potential practical applications.

Upstream product

• 962-39-0 L-Phenylalanine benzyl ester 
• 14611-34-8 N^α,N^δ,N^ω-tris(benzyloxycarbonyl)-L-arginine 
• 74-79-3 L-arginine 
• 63-91-2 L-phenylalanine 
• 35661-40-6 N-Fmoc L-Phe 
• 187618-60-6 Nα-(9-fluorenylmethyloxycarbonyl)-Nγ-2,2,4,6,7-pentamethyldihydrobenzofuran-5-sulfonyl-L-arginine 
• 1119-34-2 L-arginine hydrochloride 
• 2149-70-4 N-nitro-L-arginine 
• 27169-20-6 (Z)-Arg(NO₂)-Phe-OMe 
• 117343-23-4 N-[N^ω-nitro-N^α-(4-nitro-benzyloxycarbonyl)-L-arginyl]-L-phenylalanine ethyl ester 
• 24127-11-5 Z-Arg(NO₂)-Phe-OEt 
• 2304-98-5 N₅-[imino(nitroamino)methyl]-N₂-[(phenylmethoxy)carbonyl]-L-ornithine 
• 13726-76-6 t-butyloxycarbonyl-L-arginine 
• 16874-17-2 L-phenylalanine tert-butyl ester 

Downstream Products

• 85313-62-8 Adpoc-L-Phe-D-Leu-L-Arg-L-Phe-NH₂ 
• 85313-58-2 t-Bumeoc-L-Phe-D-Leu-L-Arg-L-Phe-NH₂ 
• 63-91-2 L-phenylalanine 

Relevant articles and documents

Solid-Phase Synthesis of Arginine-Containing Peptides by Guanidine Attachment to a Sulfonyl Linker

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Investigations of the in-vitro metabolism of three opioid tetrapeptides by pancreatic and intestinal enzymes

The metabolism of three opioid tetrapeptides, Tyr-D-Arg-Phe-Nva-NH2, Tyr-D-Arg-Phe-Phe-NH2 and Tyr-D-Ala-Phe-Phe-NH2, was investigated in the presence of pure pancreatic enzymes (trypsin, chymotrypsin, elastase, carboxypeptidase A and carboxypeptidase B), as well as in the presence of pure carboxylesterase and aminopeptidase N. The cleavage patterns of the pure pancreatic enzymes were then compared with those found in rat and human jejunal fluid. Metabolism was also studied in homogenates from different intestinal regions (duodenum, jejunum, ileum and colon) and in enterocyte cytosol from rats. The effect of various protease inhibitors was investigated in the jejunal homogenate. The parent peptides were assayed by high-performance liquid chromatography and metabolites were identified by means of liquid chromatography-mass spectrometry. Of the pure enzymes, the quickest hydrolysis of the peptides was observed for the pancreatic enzymes chymotrypsin, trypsin and carboxypeptidase A. In most cases they formed the corresponding deamidated tetrapeptides (chymotrypsin and trypsin) or tripeptides with a missing C-terminal amino acid (carboxypeptidase A). Regional differences in intestinal metabolism rates were found for all three peptides (P A showed that lumenal pancreatic proteases might be a clear metabolic obstacle in oral delivery even for small peptides such as these tetrapeptides.

A novel L-amino acid ligase from Bacillus subtilis NBRC3134, a microorganism producing peptide-antibiotic rhizocticin

L-Amino acid ligase catalyzes the formation of an α-peptide bond from unprotected L-amino acids in an ATP-dependent manner, and this enzyme is very useful in efficient peptide production. We performed enzyme purification to obtain a novel L-amino acid lig