2874-20-6

Upstream product

• 4070-48-8 L-Valine methyl ester 
• 61350-60-5 (S)-benzyloxycarbonyl-proline acid chloride 
• 1148-11-4 N-Benzyloxycarbonyl-L-proline 
• 541-41-3 chloroformic acid ethyl ester 
• 13673-56-8 Z-Pro-OPcp 
• 6306-52-1 L-valine methylester hydrochloride 
• 26607-48-7 1-benzyl hydrogen (S)-pyrrolidine-1,2-dicarboxylate, compound with dicyclohexylamine (1:1) 
• 72-18-4 L-valine 
• 501-53-1 benzyl chloroformate 
• 147-85-3 L-proline 

Downstream Products

• 21285-27-8 (2S)-2-[({(2S)-1-[(benzyloxy)carbonyl]tetrahydro-1H-pyrrol-2-yl}carbonyl)amino]-3-methylbutanoic acid 
• 52899-09-9 N-L-prolyl-L-valine 
• 119622-15-0 N⁶-benzyloxycarbonyl-N²-[N-(1-benzyloxycarbonyl-L-prolyl)-L-valyl]-L-lysine-methyl ester 
• 121075-28-3 N⁶-benzyloxycarbonyl-N²-[N-(1-benzyloxycarbonyl-L-prolyl)-L-valyl]-L-lysine 
• 73871-00-8 Z-D-Phe-L-Pro-L-Val-OMe 
• 2854-40-2 cyclo-L-prolyl-L-valine 

Relevant academic research and scientific papers

Borinic acid catalysed peptide synthesis

The catalytic synthesis of peptides is a major challenge in the modern organic chemistry hindered by the well-established use of stoichiometric coupling reagents. Herein, we describe for the first time that borinic acid is able to catalyse this reaction under mild conditions with an improved activity compared to our recently developed thiophene-based boronic acid. This catalyst is particularly efficient for peptide bond synthesis affording dipeptides in good yields without detectable racemization.

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.

N,N'-Bis(2-oxo-3-oxazolidinyl)phosphorodiamidic Azide: A Useful Coupling Agent in Peptide Synthesis

N,N'-Bis(2-oxo-3-oxazolidinyl)phosphorodiamidic azide (BOPA), has been developed as an efficient coupling reagent in peptide synthesis.Coupling reaction proceeds smoothly with no detectable racemization.

RATES OF PEPTIDE FORMATION INVOLVING IMINO ACID RESIDUES

The determination of the rates for peptide coupling in tetrahydrofuran between Z-Aaa-OPcp (Aaa = Ala, (NMe)Ala, Pro, Thz, Pip and (S)Pip) and H-Bbb-OMe (Bbb = (NMe)Ala, Pro, Thz, Pip and (S)Pip) allowed us to evaluate the relative reactivities between these members, either as active components or as amino components.The reactivity of Pro (either as the active species or the amino component) equals that of (NMe)Ala.The reactivity of Pip and (S)Pip as imino components is low while the activation energy is raised by an amount that roughly equals the energy increment needed for bringing the carboxylate grouping from the equatorial to the axial position The reactivities of these six-membered residues are also appreciably low when being the active components during peptide coupling.The presence of a ring-sulfur atom at γ-position of nitrogen additionally decreases the rate for peptidation, especially if (S)Pip is the imino component.