3005-89-8

Upstream product

• 2018-66-8 Z-Leu-OH 
• 3081-24-1 H-Phe-OEt 
• 76863-45-1 (S)-benzyl (1-azido-4-methyl-1-oxopentan-2-yl)carbamate 
• 3242-70-4 Z-Leu-NHNHPh 
• 3182-93-2 (L)-phenylalanine ethyl ester hydrochloride 
• 1795-96-6 phenylalanine ethyl ester 
• 28862-79-5 Z-D-Leu-OH 
• 543-27-1 isobutyl chloroformate 

Downstream Products

• 3063-05-6 Leu-Phe-OH 
• 74973-89-0 N-L-leucyl-L-phenylalanine ethyl ester; hydrochloride 
• 13171-96-5 Cbz-Leu-Phe-NH₂ 
• 6401-63-4 N-benzyloxycarbonyl-L-leucyl-L-phenylalanine 
• 16817-66-6 benzyl ((S)-1-(((S)-1-hydrazinyl-1-oxo-3-phenylpropan-2-yl)amino)-4-methyl-1-oxopentan-2-yl)carbamate 

Relevant academic research and scientific papers

Peptide Bond Formation via Nα-Protected Diacyldiselenides

Abstract: A simple, straightforward, for the peptide bond formation employing corresponding carboxylic acids and amines derived from amino acids via Nα-protected diacyldiselenide is delineated. The key step of the synthesis is the in situ gener

Amide and Peptide Bond Formation in Water at Room Temperature

A general and environmentally responsible method for the formation of amide/peptide bonds in an aqueous micellar medium is described. Use of uronium salt (1-cyano-2-ethoxy-2-oxoethylidenaminooxy)dimethylaminomorpholinocarbenium hexafluorophosphate (COMU) as a coupling reagent, 2,6-lutidine, and TPGS-750-M represents mild conditions associated with these valuable types of couplings. The aqueous reaction medium is recyclable leading to low E Factors.

Phosphonyldipeptides useful in the treatment of cardiovascular diseases

Compounds of formula (II) STR1 wherein R is a biphenyl group optionally substituted by one or more substituents, the same or different, selected among halogen atoms, hydroxy groups, alkoxy, alkyl or thioalkyl groups having from 1 to 6 carbon atoms in the

Selectivity and Specificity in Substrate Binding to Proteases: Novel Hydrolytic Reactions Catalysed by α-Chymotrypsin Suspended in Organic Solvents with Low Water Content and Mediated by Ammonium Hydrogen Carbonate

α-Chymotrypsin suspended in organic solvents with low water content catalysed hydrolytic reactions in the presence of ammonium hydrogen carbonate.Molecular modelling studies were carried out and structure-reactivity relationships were established by studying the hydrolysis of amino acid derivatives and analogues.The enzyme was found to be stereoselective with respect to the hydrolysis of L-amino acid derivatives, but no stereoselectivity was observed when α-hydroxy esters were used as substrates.A general procedure for the resolution of aromatic amino acid esters is given.The results are interpreted in terms of molecular modelling based on X-ray crystallographic data and literature data.