Enzymatic Peptide Synthesis in Frozen Aqueous Solution: Use of Nα-unprotected Peptide Esters as Acyl Donors

✍ Scribed by Sabine Gerisch; Hans-Dieter Jakubke

• Publisher: John Wiley and Sons
• Year: 1997
• Tongue: English
• Weight: 84 KB
• Volume: 3
• Category: Article
• ISSN: 1075-2617
• DOI: 10.1002/(sici)1099-1387(199703)3:2<93::aid-psc87>3.0.co;2-r

✦ Synopsis

The ability of the endopeptidase a-chymotrypsin (EC 3.4.21.1) to catalyse the reaction of various N aunprotected di-and tripeptide ester derivatives with H-Leu-NH 2 , and with a series of C-terminal free di-and tripeptides at ÿ15 C in frozen aqueous solution was investigated. The enzyme is able to synthesize N-and Cterminal unprotected penta-and hexapeptides in up to 92% yield, depending on the amino component used, in a single-step segment-condensation reaction. Freezing the reaction mixture resulted in significantly increased peptide yields compared with the reaction at room temperature. The enzyme shows a modified nucleophilic specificity in frozen solution compared with room temperature. Nucleophilic amino components with positively charged amino acids in P 2 0 -position are accepted.