181117-83-9

Upstream product

• 15761-38-3 L-N-Boc-Ala 
• 181117-79-3 4-[N',N''-bis(benzyloxycarbonyl)guanidino]phenol 
• 152120-55-3 N,N-bis(benzyloxycarbonyl)-1H-pyrazole-1-carboxamidine 
• 2483-49-0 tert-butyloxycarbonyl-L-alanine p-nitrophenyl ester 
• 123-30-8 4-amino-phenol 
• 100-02-7 4-nitro-phenol 

Relevant academic research and scientific papers

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).

Synthesis and tryptic hydrolysis of p-guanidinophenyl esters derived from amino acids and peptides

A facile synthetic method for p-guanidinophenyl esters derived from a variety of amino acids and peptides, including D-amino acids, is presented. The kinetic behavior of trypsin towards these synthetic esters, inverse substrates, was analyzed. The spatial