83703-83-7

Upstream product

• 67-56-1 methanol 
• 93936-31-3 Cbz-Val-Ala-NH₂ 
• 2491-20-5 L-alanine methyl ester hydrochloride 
• 133010-20-5 Cbz-Val-F 
• 501-53-1 benzyl chloroformate 
• 72-18-4 L-valine 
• 1149-26-4 (S)-N-(benzyloxycarbonyl)valine 
• 54647-77-7 N-[(benzyloxy)carbonyl]-L-valine, compound with dicyclohexylamine (1:1) 
• 10065-72-2 L-Alanine methyl ester 

Downstream Products

• 77834-25-4 Z-Ile-Val-Ala-OMe 
• 1361509-39-8 (S)-methyl 2-((S)-2-(benzyloxycarbonylamino)-3-methylbutaneselenoamido)propanoate 
• 17445-33-9 (S)-2-((S)-2-(((benzyloxy)carbonyl)amino)-3-methylbutanamido)propanoic acid 
• 16816-23-2 N-(benzyloxycarbonyl)-L-leucyl-L-valcyl-L-alanine methyl ester 
• 80165-13-5 {(S)-1-[(S)-1-((S)-1-Carbamoyl-3-methyl-butylcarbamoyl)-ethylcarbamoyl]-2-methyl-propyl}-carbamic acid benzyl ester 
• 77834-27-6 Z-Ile-Ile-Val-Ala-NHNH₂ 
• 77834-26-5 Z-Ile-Ile-Val-Ala-OMe 

Relevant academic research and scientific papers

Ethyl propiolate: A simple and convenient peptide coupling reagent

Ethyl propiolate has been used to activate N-protected amino acids to form a moderately activated vinyl-ester which aminolysis requires a catalytic amount of sodium bisulfite.

Metal-free approach for hindered amide-bond formation with hypervalent iodine(iii) reagents: application to hindered peptide synthesis

A new bio-inspired approach is reported for amide and peptide synthesis using α-amino esters that possess a potential activating group (PAG) at the ester residue. To activate the ester functionality under mild metal-free conditions, we exploited the facile dearomatization of phenols with hypervalent iodine(iii) reagents. Using a pyridine-hydrogen fluoride complex, highly reactive acyl fluoride intermediates can be successfully generated, thereby allowing for the smooth formation of sterically hindered amides and peptides from bulky amines and α-amino esters, respectively.

Synthesis of selenoxo peptides and oligoselenoxo peptides employing LiAlHSeH

Synthesis of selenoxo peptides by the treatment of Nα- protected peptide esters with a combination of PCl5 and LiAlHSeH is delineated. The method is simple, high-yielding, and free from racemization. Thus obtained selenoxo peptides are used as units for N-terminal chain extension through Nα-deprotection/coupling to yield peptide-selenoxo peptide hybrids. Multiple selenation is demonstrated by conversion of two peptide bonds of tripeptides into selenoxo peptide bonds. Amino acid derived arylamides are also converted into aryl selenoamides. C6H 5-CSeNH-Val-OMe 8f is obtained as single crystal, and its structure was determined through X-ray diffraction study.

Fully enzymatic N→C-directed peptide synthesis using C-terminal peptide α-carboxamide to 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 and racemisation does not occur rendering purification easier compared to chemical peptide synthesis. In this paper, a novel interconversion reaction of peptide C-terminal α-carboxamides into primary alkyl esters with alcalase was used to develop a fully enzymatic peptide synthesis strategy. For each elongation step a cost-efficient amino acid carboxamide building block was used followed by the interconversion of the elongated peptide carboxamide to the corresponding primary alkyl ester. These peptide esters are the starting materials for the next enzymatic peptide elongation step. Copyright

N-tert-Butylglyoxylicamide, the New Reagent for Peptide Segment Coupling by Four-Component Reaction

In contrast to the use of other aldehyd components, the Tetra Component Reactions (4CR) of carboxyl acids and primary amines with combinations of N-tert-butylglyoxylicamide and isocyanides produce carbonamides that yield the desired stereochemically unifo

KINETICS OF THE ALKALINE HYDROLYSIS OF SEVERAL N-BENZYLOXYCARBONYLDIPEPTIDE METHYL AND ETHYL ESTERS

The reaction rates of the alkaline hydrolysis of synthesized N-protected dipeptide methyl and ethyl esters were studied systematically.From the kinetic data the energies of activation, the pre-exponential factors and the reference values at 40 deg C were calculated.The rate of hydrolysis shows to be strongly dependent on the C-terminal amino acid in the sequence Gly >> Ala/Met/Phe > Leu >> Val/Pro.Surprisingly the N-terminal amino acid also exerts an effect, but in a different sequence.N-Terminal Phe in particular shows a relative accelerating effect.Remarkable is the significantly faster ester hydrolysis of glycine containing dipeptide ethyl esters in ethanol/water compared to the corresponding methyl esters in methanol/water.