71450-10-7

Upstream product

• 4510-08-1 L-methioninamide 
• 60117-24-0 H-Tyr-Gly-Gly-Phe-Leu-NH₂ 
• 84969-58-4 Met-NH₂*HCOOH 
• 3065-27-8 benzyloxycarbonyl-L-phenylalanine 2,4,5-trichlorophenyl ester 
• 545390-94-1 Z-Phe-SMe 
• 13126-07-3 Cbz-L-Phe-L-Met-OH 
• 4816-89-1 Cbz-Phe-OCH₂CONH₂ 
• 16120-92-6 (S)-methioninamide hydrochloride 
• 928787-83-1 Cbz-L-Phe-L-Met-Bt 
• 1161-13-3 N-Cbz-L-Phe 

Downstream Products

• 71450-13-0 L-Phe-L-Met-NH₂ formate 
• 63-68-3 L-methionine 
• 63-91-2 L-phenylalanine 

Relevant academic research and scientific papers

Convenient primary amidation of N-protected phenylglycine and dipeptides without racemization or epimerization

Primary amidation of N-protected phenylglycine and dipeptide proceeded easily to afford the corresponding amides in 57-95% yields with 99% ee and 81-99% de, respectively. The procedure is very easy to avoid racemization and epimerization of the products in the reactions by keeping exactly the reaction temperature at -15 C when the activation of carboxylic acids, followed by the reaction of the mixed carbonic carboxylic anhydride with NH4Cl.

Kinetically controlled peptide synthesis mediated by papain using the carbamoylmethyl ester as an acyl donor

A series of dipeptides were synthesized generally in good yields with carbamoylmethyl (Cam) esters as acyl donors in the presence of a cysteine protease, papain, immobilized on Celite. Several segment condensations were also achieved generally in high yields without danger of racemization and formation of the secondary-hydrolysis product. Moreover, partial sequences of some bioactive peptides were prepared through segment condensations, and aimed-at peptides were obtained generally in high yields without the racemization of C-terminal residues of the carboxyl components. Thus, the superiority of the Cam ester in the kinetically controlled peptide synthesis was once again ascertained in couplings mediated by the cysteine protease as in those catalyzed by the serine proteases reported earlier.

Convenient synthesis of C-terminal di- and tri-peptide amides from N-protected dipeptidoylbenzotriazoles

N-Protected dipeptidoylbenzotriazoles react with aqueous ammonia to give dipeptide primary amides (77-98%) and with N-unprotected α-amino amides to afford tripeptide primary amides (82-86%).

Reverse proteolysis promoted by in situ generated peptide ester fragments

In this contribution we describe a general synthesis concept for the in situ preparation of protease specific reactants using methyl thioesters as universal precursors. The precursor esters are readily available by standard synthesis procedures and can be

Pronase catalysed peptide syntheses

A mixture of proteases from Streptomyces griseus (pronase), displaying a very broad substrate tolerance in the hydrolysis of peptides, has been studied for the first time systematically regarding their substrate specificity in peptide synthesis. It is demonstrated that pronase can be employed successfully for the formation of dipeptides with yields up to 95%. Pronase has also been employed successfully as catalyst for the enzyme assisted synthesis of a hexapeptide.

Catalytic Transfer Hydrogenation in Pepetide Synthesis: Synthesis of 5- and 5-enkephalins

The simplicity in the removal of N-protecting groups like benzyloxycarbonyl employed in peptide synthesis by catalytic transfer hydrogenation at room temperature using formic acid in presence of palladium black has been demonstrated by the synthesis of the opioid pentapeptides 5- and 5-enkephalins.