2953-42-6

Usage

Uses

Used in Pharmaceutical Industry:
L-Leucine, N-[(phenylmethoxy)carbonyl]-L-phenylalanyl-, ethyl ester is used as a building block in peptide synthesis for the creation of biologically significant peptides. These peptides are crucial in the development of new drugs and pharmaceuticals, as they can be engineered to have specific therapeutic properties.
Used in Research and Development:
In the field of medicine and biochemistry, L-Leucine, N-[(phenylmethoxy)carbonyl]-L-phenylalanyl-, ethyl ester is utilized in research and development to explore its potential to modify and enhance the properties of peptides and proteins. This can lead to advancements in understanding the structure and function of these molecules, as well as the discovery of new therapeutic applications.

Upstream product

• 2743-40-0 L-leucine ethyl ester hydrochloride 
• 64-17-5 ethanol 
• 29842-94-2 (S)-tert-butyl 2-((S)-2-(((benzyloxy)carbonyl)amino)-3-phenylpropanamido)-4-methylpentanoate 
• 58889-73-9 (S)-N-benzyloxycarbonyl-leucine ethyl ester 
• 1161-13-3 N-Cbz-L-Phe 
• 2743-60-4 L-Leucine ethyl ester 
• 3397-32-8 N-(benzyloxycarbonyl)-phenylalanine-N-hydroxysuccinimide ester 

Downstream Products

• 3982-72-7 Cbz-Gly-L-Phe-L-Leu-OEt 
• 3354-31-2 (3S,6S)-3-benzyl-6-isobutylpiperazine-2,5-dione 
• 60566-42-9 L-phenylalanyl-L-leucine ethyl ester 

Relevant academic research and scientific papers

Tandem deprotection/coupling for peptide synthesis in water at room temperature

A tandem deprotection/coupling sequence is reported for solution-phase peptide synthesis in water under micellar catalysis conditions using the designer surfactant TPGS-750-M. Cbz deprotection followed by peptide coupling in the presence of COMU and 2,6-lutidine afforded polypeptides containing up to 10 amino acid residues. A broad scope characterizes this new technology. No epimerization has been detected. The associated E Factors, as a measure of "greenness" and known to be extremely high for peptide couplings, have been reduced to less than 10 due to the step-economy and minimal amounts of organic solvent needed for product extraction.

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.

Fully enzymatic peptide synthesis using C-terminal tert-butyl ester interconversion

Chemoenzymatic peptide synthesis is potentially the most cost-efficient technology for the synthesis of short and medium-sized peptides with some important advantages. For instance, stoichiometric amounts of expensive coupling reagents are not required an

An improved method for the synthesis of active esters of N-protected amino acids and subsequent synthesis of dipeptides

4-Dimethylaminopyridine-catalyzed reaction of mixed carbonates 3 with N-protected amino acids 4 gave the corresponding active esters 5-9, from which dipeptides 11-18 were synthesized by aminolysis with amino acids 10.