85697-77-4Relevant academic research and scientific papers
Trypsin-catalyzed synthesis of dipeptide containing α-aminoisobutylic acid using p- and m-(amidinomethyl)phenyl esters as acyl donor
Sekizaki, Haruo,Itoh, Kunihiko,Shibuya, Akiyoshi,Toyota, Eiko,Kojoma, Mareshige,Tanizawa, Kazutaka
, p. 688 - 691 (2008)
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.
Atlantic cod trypsin-catalyzed peptide synthesis with inverse substrates as acyl donor components
Fuchise, Tomoyoshi,Kishimura, Hideki,Yang, Zhi-Hong,Kojoma, Mareshige,Toyota, Eiko,Sekizaki, Haruo
experimental part, p. 484 - 487 (2010/08/19)
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.
Methyltrypsin-catalyzed peptide coupling: Comparison of alkyl ester and guanidinophenyl ester derivatives as acyl donor component
Itoh, Kunihiko,Sekizaki, Haruo,Toyota, Eiko,Tanizawa, Kazutaka
, p. 307 - 319 (2007/10/03)
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
Sekizaki, Haruo,Itoh, Kunihiko,Toyota, Eiko,Tanizawa, Kazutaka
, p. 1585 - 1587 (2007/10/03)
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
