Asymmetric catalysis at a distance: catalytic, site-selective phosphorylation of teicoplanin.

ABSTRACT: We report three distinct, peptide-based catalysts that enable site-selective phosphorylation of three distinct hydroxyl groups within the complex glycopeptide antibiotic teicoplanin A2-2. Two of the catalysts are based on a design that capitalizes on a catalyst-substrate interaction that mimics the biological mechanism of action for teicoplanin. These catalysts are based on a DXaa-DXaa peptide motif that is known to target the teicoplanin structure in a specific manner. The third was identified through evaluation of a set of catalysts that had been developed for historically distinct projects. Each catalyst contains additional functionality designed to dispose a catalytic moiety (a nucleophilic alkylimidazole) at a different region of the glycopeptide structure. A combination of mass spect

SUBMITTER: Han S 

PROVIDER: S-EPMC3790668 | biostudies-literature | 2013 Aug

REPOSITORIES: biostudies-literature