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Enzyme-labile protecting groups in peptide synthesis: Development of glucose- and galactose-derived urethanes

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http://pubman.mpdl.mpg.de/cone/persons/resource/persons98735

Waldmann,  Herbert
Abt. IV: Chemische Biologie, Max Planck Institute of Molecular Physiology, Max Planck Society;

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Gum, A., Kappes-Roth, T., & Waldmann, H. (2000). Enzyme-labile protecting groups in peptide synthesis: Development of glucose- and galactose-derived urethanes. CHEMISTRY-A EUROPEAN JOURNAL, 6(20), 3714-3721. doi:10.1002/1521-3765(20001016)6:20<3714:AID-CHEM3714>3.0.CO;2-Z.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0014-6F05-0
Abstract
The development of the tetra-O-acetyl-D-glucopyranosyloxycarbonyl (AGlOC) and tetra-O-acetyl-beta -D-galactopyranosyloxycarbonyl (AGalOC) protecting groups, which are fully enzymelabile, carbohydrate-derived urethanes, is described. The protected amino acids were easily synthesized and subsequently converted into a series of model dipeptides through classical peptide couplings. Cleavage of an alpha/beta -anomeric mixture of a model AGlOC dipeptide was achieved with a "one-pot" procedure in good yield. To gain a better understanding of the enzymatic deprotection reaction, the AGalOC group was removed through a two step biotransformation (lipase catalyzed deacetylation, followed by beta -galactosidase catalyzed glycosidic bond fragmentation). Under these very mild reaction conditions tag. buffer pH 7.0, 37 degreesC), the desired N-terminal, unprotected dipeptide conjugates were obtained. The methodology was further utilized for the synthesis of an advanced tetrapeptide model system.