102292-84-2

Upstream product

• 3744-87-4 Boc-(R)-Ala 
• 77286-89-6 Ala-pNA 
• 102292-83-1 Z-D-Ala-pNA 
• 100-01-6 4-nitro-aniline 
• 1027047-37-5 C₃₂H₃₆N₄O₈ 

Downstream Products

• 99242-11-2 Suc-L-Ala-D-Ala-D-Ala-pNA 
• 60354-61-2 H-L-Ala-D-Ala-D-Ala-pNA 
• 50439-37-7 Boc-L-Ala-D-Ala-D-Ala-pNA 
• 783263-76-3 H-D-Ala-D-Ala-pNA 

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.

Enzymatic peptide synthesis with p-guanidinophenyl and p- (guanidinomethyl)phenyl esters as acyl donors

Two series of 'inverse substrates', N-Boc-amino acid p-guanidinophenyl and p-(guanidinomethyl)phenyl esters, were prepared as acyl donor components for enzymatic peptide synthesis. The kinetic behavior of these esters toward bovine and Streptomyces griseus (SG) trypsin was analyzed. The spatial requirement of the active site of these enzymes for catalytic efficiency is discussed based on the steric characteristics of the substrates. These substrates were found to couple readily with amino acid p-nitroanilides to produce peptides. SG trypsin was the most efficient catalyst among the enzymes tested (bovine, porcine, and SG trypsin).