110392-41-1

Basic information

• Product Name: L-Argininamide, N-acetyl-L-phenylalanyl-
• CAS NO: 110392-41-1
• Molecular Formula: C17H26N6O3
• Molecular Weight: 362.432
• Mol File: 110392-41-1.mol
• Article Data: 3

Chemical Properties

• CAS DataBase Reference: L-Argininamide, N-acetyl-L-phenylalanyl-(CAS DataBase Reference)
• NIST Chemistry Reference: L-Argininamide, N-acetyl-L-phenylalanyl-(110392-41-1)
• EPA Substance Registry System: L-Argininamide, N-acetyl-L-phenylalanyl-(110392-41-1)

Safety Data

• Hazardous Substances Data: 110392-41-1(Hazardous Substances Data)

Upstream product

• 13734-34-4 N-tert-butoxycarbonyl-L-phenylalanine 
• 13836-37-8 Boc-Arg(Tos)-OH 
• 108-24-7 acetic anhydride 
• 814263-53-1 (2S)-2-N-(9-fluorenylmethyloxycarbonyl)amino-5-isothiocyanatopentanamide 
• 35661-40-6 N-Fmoc L-Phe 
• 64-19-7 acetic acid 
• 119158-02-0 Fmoc-L-Orn-NH₂ 
• 109425-55-0 Fmoc-Orn(Boc)-OH 
• 119158-01-9 Fmoc-L-Orn(Nδ-Boc)-NH2 
• 2466-76-4 N-Acetylimidazole 

Relevant articles and documents

Solid-phase synthesis of arginine-containing peptides and fluorogenic substrates using a side-chain anchoring approach

Attachment of an amino acid to a solid support by its side chain is sometimes necessary to take advantage of an α-carboxylic group available for diverse modifications, including the incorporation of a fluorophore for the preparation of fluorogenic substrates. In contrast to most other amino acids, anchoring the guanidinium group of an arginine to a resin requires the use of a supplementary linker. To avoid the usually multistep synthesis of such a linker as well as its difficult attachment to the guanidine group, we developed a simple method where the guanidine group is built on a Rink amide resin. Our strategy followed the steps of guanidine formation: (i) addition of an isothiocyanate derivative of ornithine to the amino group of a solid support, yielding Nω-linked thiocitrulline; (ii) S-methylation of thiourea; (iii) guanidinylation using ammonium acetate. Cleavage of the resin generated the arginine-containing compound, the amine group of the resin becoming part of the guanidine. We have demonstrated the usefulness of this method by the synthesis of a series of fluorogenic substrates for trypsin-like serine proteases, which were obtained in high yield and purity. Then, our strategy also allowed generation from the same precursor differentially substituted arginine derivatives, including Nω-methyl- and Nω-ethylarginines. The ability to prepare such analogues together with the intermediates thiocitrulline and S-methylisothiocitrulline from a unique precursor while the α-amine and carboxylic groups remain available for modification also makes this method a powerful tool for combinatorial solid-phase synthesis of NO synthase inhibitors.

α-Melanotropin: The Minimal Active Sequence in the Frog Skin Bioassay

The minimal sequence required for biological activity of α-MSH (α-melanotropin, α-melanocyte stimulating hormone) was determined in the frog (Rana pipiens) skin bioassay.The sequence required to elicit measurable biological activity was the central tetrap