A facile Fmoc solid phase synthesis strategy to access pimerization-prone 
biosynthetic intermediates of glycopeptide antibiotics

Brieke, Clara; Cryle, Max

doi:10.1021/ol500840f

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A facile Fmoc solid phase synthesis strategy to access pimerization-prone biosynthetic intermediates of glycopeptide antibiotics

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Brieke, Clara
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Cryle, Max
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;
Cytochrome P450, Max Planck Institute for Medical Research, Max Planck Society;

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Citation

Brieke, C., & Cryle, M. (2014). A facile Fmoc solid phase synthesis strategy to access pimerization-prone biosynthetic intermediates of glycopeptide antibiotics. Organic Letters, 16(9), 2454-2457. doi:10.1021/ol500840f.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0019-8F83-1

Abstract

A rapid protocol based on Fmoc-chemistry for the solid phase peptide synthesis of vancomycin- and teicoplanin-type peptides is described. Epimerization of highly racemization-prone arlyglycine derivatives is suppressed through optimized Fmoc-deprotection and coupling conditions. Starting from easily accessible Fmoc-protected amino acids, this strategy enables the enantioselective synthesis of peptides corresponding to intermediates found in vancomycin and teicoplanin biosynthesis with excellent purity and in high yields (38%–71%).