Enzymatic Cleavage of tert-Butyl Esters: Thermitase-Catalyzed Deprotection of Peptides and O-Glycopeptides

Michael Schultz; Peter Hermann; Horst Kunz

doi:10.1055/s-1992-21257

Synlett 1992; 1992(1): 37-38
DOI: 10.1055/s-1992-21257

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Enzymatic Cleavage of tert-Butyl Esters: Thermitase-Catalyzed Deprotection of Peptides and O-Glycopeptides

Michael Schultz^* , Peter Hermann, Horst Kunz

^*Institut für Organische Chemie, Universität Mainz, Becherweg 18-20, D-6500 Mainz, Germany

Abstract

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The tert-butyl esters of differently N-protected peptides are selectively cleaved in a thermitase-catalyzed reaction without affecting the peptide bonds. Furthermore, an O-glycopeptide carrying a N-acetylglucosamine side chain readily undergoes the same selective deblocking reaction, thus demonstrating the broad scope of this method.

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