82518-66-9

Upstream product

• 4530-20-5 BOC-glycine 
• 1668-13-9 L-alanine-p-nitroanilide 
• 1050507-37-3 N-(tert-butoxycarbonyl)glycine p-(amidinomethyl)phenyl ester p-toluenesulfonic acid salt 
• 181117-96-4 4-guanidinophenyl N-(tert-butoxycarbonyl)glycinate 

Downstream Products

• 66493-44-5 2-(2-amino-acetylamino)-N-(4-nitro-phenyl)-propionamide 

Relevant academic research and scientific papers

Atlantic cod trypsin-catalyzed peptide synthesis with inverse substrates as acyl donor components

Atlantic cod trypsin-catalyzed peptide synthesis has been studied by using p-amidino- and p-guanidinophenyl esters of N-(tert-butyloxycarbonyl)amino acid as acyl donor components. The reaction temperature was optimized at 0 °C. The method was shown to be successful as effectively for synthesizing the peptide and useful for preparing dipeptide between D-amino acid with D-amino acid and β-amino acid with β-amino acid, respectively. The enzymatic hydrolysis of the resulting products was negligible.

Trypsin-catalyzed synthesis of dipeptide containing α-aminoisobutylic acid using p- and m-(amidinomethyl)phenyl esters as acyl donor

Two series of inverse substrates, p- and m-(amidinomethyl)phenyl esters derived from N-(tert-butyloxycarbonyl) amino acid, were prepared as acyl donor components for enzymatic peptide synthesis. They were found to be readily coupled with an acyl acceptor such as L-alanine p-nitroanilide to produce dipeptide. An α-aminoisobutyric acid containing dipeptide was especially obtained in satisfactory yield. Streptomyces griseus trypsin was a more efficient catalyst than the bovine trypsin. The optimum condition for the coupling reaction was studied by changing the organic solvent, pH, and acyl acceptor concentration. It was found that the enzymatic hydrolysis of the resulting product was negligible.

Polymer-assisted solution-phase parallel synthesis of dipeptide p-nitroanilides and dipeptide diphenyl phosphonates

This letter describes the parallel synthesis of dipeptide p-nitroanilides (1) and dipeptide diphenyl phosphonates (2), compounds that can be used as substrates and irreversible inhibitors for the rapid profiling of dipeptidyl peptidases. A polymer-assisted solution-phase synthesis was used for a rapid and clean coupling between easily available building blocks.

Methyltrypsin-catalyzed peptide coupling: Comparison of alkyl ester and guanidinophenyl ester derivatives as acyl donor component

Methyltrypsin-catalyzed peptide synthesis has been studied by using conventional alkyl ester and p-guanidinophenyl ester derivatives of α-amino acid as the acyl donor component. They were found to be coupled with α- amino acid derivatives (acyl acceptor component) to produce dipeptide. The behavior of methyltrypsin toward both the substrates has been studied.

Trypsin-catalyzed peptide synthesis with various p-guanidinophenyl esters as acyl donors

Trypsin-catalyzed peptide synthesis has been studied by using p- guanidinophenyl esters of N(α)-(tert-butyloxycarbonyl)amino acid and peptide as acyl donor components. The reaction conditions were optimized for organic solvents, pH, and concentration of a

Application of inverse substrates to trypsin-catalyzed peptide synthesis

Trypsin-catalyzed peptide synthesis has been studied by using 'inverse substrate,' i.e., p-amidinophenyl ester derived from α-amino acid derivative as an acyl donor component. Inverse substrate can afford acyl trypsin in a very specific manner, liberating

Upon DNP-aromatic Rule. Effect of Chromophore Exchange on the CD Spectra of N-DNP-arylalkylamines

CD spectra of the analogs of aromatic DNP-α-amino acids and the related N-DNP-arylalkylamines, in which the positions of the two chromophoric groups were exchanged with each other, were studied.The analogs, in which the DNP-amino group is separated from the asymmetric carbon, did not show any marked Cotton effect near 400 nm, indicating the importance of direct attachment of the DNP-NH group to the chiral carbon atom for showing the characteristic CD spectra of N-DNP-aromatic α-amino acids.