61884-21-7

Upstream product

• 35446-34-5 N-acetyldehydrophenylalanyl-S-proline 
• 147-85-3 L-proline 
• 2018-61-3 (S)-2-acetylamino-3-phenylpropanoic acid 
• 65941-28-8 N-acetyl-α,β-dehydrophenylalanyl-(S)-proline 
• 100-52-7 benzaldehyde 
• 881-90-3 4-benzylidene-2-methyl-2-oxazolin-5-one 

Relevant academic research and scientific papers

Complexation equilibrium in a substrate - MgCl2(CaCl2) - Pd/c catalytic system and the influence of its position on asymmetric induction in hydrogenation of N-acetyl-dehydrophenylalanyl-S-proline

The role of Ca and Mg salts as promoters of asymmetric induction in hydrogenation of N-acetyl-dehydrophenylalanyl-S-proline in a substrate - MX2 - Pd/C catalytic system was studied. The data of potentiometric titration, 1H NMR spectroscopy, and the value of diastereomeric excess (de) of the resulting N-acetyl-R-phenylalanyl-S-proline indicate the complexation of the substrate with calcium and magnesium chlorides in an alcoholic solution. Ionization and equilibrium constants of the complex were determined. Excess salt shifts the equilibrium toward the complex formation, which increases de up to 70 %.

Deprotonation of the peptide NH groups and diastereoselective hydrogenation of N-acetyl-α,β-dehydrodipeptides

The peptide protons in N-acetyl-α,β-dehydrodipeptides (DHDP) dissociate in aqueous methanol in the presence of magnesium salts upon the addition of alkali, which favors the diastereoselectivities of their hydrogenation over Pd/C. By contrast, the N-H bond

Complexes of Ca2+ and Mg2+ with N-acetyl-α,β-dehydrodipeptides: The state in an alcoholic solution and its relationship with asymmetric induction upon diastereoselective hydrogenation

In an alcoholic solution, N-acetyl-α,β-dehydrodipeptides interact with Ca2+ and Mg2+ ions to form complex particles containing several dehydrodipeptide molecules per metal ion. The composition of these particles and steric interactions in them determine the acidity of the carboxyl groups and the degree of asymmetric induction upon diastereoselective hydrogenation.

One step synthesis of inverted aspartame type sweetener, Ac-Phe-Lys, using chemically modified chymotrypsin

To search for techniques of simplified peptide synthesis, benzyloxycarbonyl chymotrypsin was prepared by a water-soluble acylating reagent and used to make Ac-Phe-Lys, an artificial peptide sweetener, which was selected as a target compound. As a result o

Asymmetric hydrogenation of N-acetylhydrodipeptide complexes with Mg(II) and C(II) ions

N-Ac-Δ-Phe-AA form labile complexes with Mg(II) ions.Potentiometric titration data show that the carboxyl group of the dehydropeptide in them scarcely participates in complexation, unlike the complexes with Ca(II) ions.The hydrogenation of these complexes

REACTION OF N-ACETYLDEHYDROPHENYLALANYL-S-PROLINE WITH Ca(II) AND Ni(II) IONS AND ITS ROLE IN ASYMMETRIC HYDROGENATION

N-Ac-ΔPhe-S-Pro forms strong coordination complexes with the CO2H group of the proline residue and weak coordination complexes through the -C(=O)-N groups with Ca(II) and Ni(II) ions in 95percent aqueous methanol as indicated by the pKa values,

Characteristics of chymotrypsin modified with water-soluble acylating reagents and its peptide synthesis ability in aqueous organic media.

Several kinds of modified chymotrypsin were prepared with water-soluble acylating reagents, and their characteristics after hydrolyzing with unmodified chymotrypsin in aqueous-N,N'-dimethylformamide (DMF) media were compared. It was found that chymotrypsi