108147-48-4

Upstream product

• 17186-36-6 N-Benzyloxycarbonyl-(β-O-benzyl-L-asparagyl)-L-phenylalanin-benzylester 
• 5241-71-4 Asp-Phe-NH₂ 
• 22839-47-0 L-Asp-L-Phe-OMe 
• 116147-62-7 n-formyl-l-aspartic anhydride 
• 63-91-2 L-phenylalanine 
• 962-39-0 L-Phenylalanine benzyl ester 
• 2577-90-4 L-phenylalanine methyl ester 
• 56633-51-3 N-formyl-L-α-aspartyl-L-phenylalanine 

Downstream Products

• 7732-18-5 water 
• 55102-13-1 3-benzyl-6-carboxymethyl-2,5-diketopiperazine 
• 85412-56-2 methyl 3-(1-(methoxycarbonyl)-2-phenylethylcarbamoyl)-3-aminopropanoate 
• 952313-02-9 acryloyl N-α-L-aspartyl-L-phenylalanine di-methyl ester 
• 56-84-8 L-Aspartic acid 
• 63-91-2 L-phenylalanine 
• 175176-52-0 L-valyl-L-aspartyl-L-phenylalanine 
• 22839-47-0 L-Asp-L-Phe-OMe 

Relevant academic research and scientific papers

Increased stability of peptidesulfonamide peptidomimetics towards protease catalyzed degradation

Replacement of amide bonds in peptides by sulfonamide moieties resulted in peptidosulfonamides with an increased stability towards protease catalyzed degradation. In addition to protection of the protease cleavage site, it was found that introduction of a sulfonamide also influenced the stability of adjacent amide bonds. Copyright (C) 1999 Elsevier Science Ltd.

Investigations on the degradation of aspartame using high-performance liquid chromatography/tandem mass spectrometry

Aspartame is a widely used sweetener, the long-term safety of which has been controversial ever since it was accepted for human consumption. It is unstable and can produce some harmful degradation products under certain storage conditions. A high-performa

Covalent capture purification of polypeptides after SPPS via a linker removable under very mild conditions

The covalent purification of polypeptides possessing an N-terminal cysteine or threonine residue via formation of a thiazolidine or oxazolidine with an aldehyde-functionalized-resin has been successfully demonstrated. To extend the applicability of this approach to any possible N-terminal residue, a special linker derived from (S)-4-amino-2-hydroxy-butyric acid was incorporated into peptidyl-resin. This linker represents the connecting point between the capture unit (cysteine) useful for the isolation of the desired polypeptide and the desired N-terminus. The target polypeptide was recovered by periodate oxidation, which cleaved the covalent bond between the linker and the last residue of polypeptide under very mild conditions.

Solvent effects on chemical processes. 8. Demethylation kinetics of aspartame in binary aqueous-organic solvents

The kinetics of demethylation of aspartame were studied in binary aqueous- organic solvent mixtures at 25 Γ under two solution conditions, namely 1.0 M HCI (pH 0.28 in water) and carbonate buffer (pH 10.1 in water). Under these conditions solvent effects

Preparation process of α-l-aspartyl-l-phenyl-alanine methyl ester or hydrohalide thereof

α-L-aspartyl-L-phenylalanine methyl ester or the hydrohalide thereof is prepared by esterifying α-L-aspartyl-L-phenylalanine or α-L-aspartyl-L-phenylalanine which has been formed in situ by treating an N-protected-α-L-aspartyl-L-phenylalanine in an aqueou

Process for producing α-L-aspartyl-L-phenylalanine methyl ester

A process for preparing an α-L-aspartyl-L-phenylalanine methyl ester which comprises the steps of reacting formyl-L-aspartic anhydride with L-phenylalanine in the presence of water at a high pH, to produce formyl-α-L-aspartyl-L-phenylalanine; removing the formyl group from the formyl-α-L-aspartyl-L-phenylalanine and esterifying the resultant compound with methanol and hydrogen chloride to produce the hydrogen chloride salt of α-L-aspartyl-L-phenylalanine methyl ester; neutralizing the hydrogen chloride salt of α-L-aspartyl-L-phenylalanine methyl ester; and filtering the neutralized solution to produce α-L-aspartyl-L-phenylalanine methyl ester.

Hydrolysis of esters of α-L-aspartyl-L-phenylalanine

A process which comprises contacting alkyl esters of α-L-aspartyl-L-phenylalanine with an aqueous solution containing barium ions, at a reaction pH greater than 7, to form α-L-aspartyl-L-phenylalanine.

Process for the preparation of α-L-aspartyl-L-phenylalanine alkyl esters

A process for the preparation of α-L-aspartyl-L-phenylalanine alkyl esters wherein L-phenylalanine is reacted with N-protected-L-aspartic anhydride, the resulting product is treated to yield α-L-aspartyl-L-phenylalanine which is esterified with an alkanol to yield an α-L-aspartyl-L-phenylalanine alkyl ester which is recovered. Novel precursors for α-L-aspartyl-L-phenylalanine alkyl esters are prepared in the process of this invention.