Atlantic Cod Trypsin-Catalyzed Peptide Synthesis with Inverse Substrates as Acyl Donor Components

• Published in: Chemical & Pharmaceutical Bulletin Vol. 58; no. 4; pp. 484 - 487
• Main Authors: Tomoyoshi FUCHISEa, Hideki KISHIMURAb, Zhi-hong YANGc, Mareshige KOJOMAa, Eiko TOYOTAa, Haruo SEKIZAKIa
• Format: Journal Article
• Language: Japanese
• Published: Pharmaceutical Society of Japan 2010
• ISSN: 0009-2363

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℃. 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. A large number of biologically active peptides have been isolated recently from bacterial, fungal, plant and animal sources and characterized in some detail. In particular, short-sequence peptides play important roles in the sensory appreciation of food toward four basic taste sensations (sweet, bitter, sour and salty). 1) Such peptides sometimes contain D-amino acid and other unusual amino acids. Synthetic chemistry has witnessed remarkable progress with the development of novel biologically active peptides.