Abstract
Glycopeptide antibiotics, with vancomycin as the most prominent representative, have gained considerable interest over recent years. This is due to their function as antibiotics of last resort for infections of methicillin-resistant Staphylococcus aureus (MRSA) strains. The antibiotic activity of glycopeptides is based on the high specificity of the aglycon cavity towards the N-acyl-D-Ala-D-Ala-peptide motif of bacterial cell wall precursors as summarized in recent reviews [1,2]. First insights into the glycopeptide antibiotic biosynthesis have been obtained by sequencing the chloroeremomycin gene cluster of Amycolatopsis orientalis [3] and cloning and analyzing the balhimycin cluster of Amycolatopsis mediterranei [4]. We addressed our research to understand how nature assembles the side chain-cyclized aglycon cavity, which is an essential element of a whole class of natural compounds.
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Bischoff, D. et al. (2001). Shedding Light on the Aglycon Formation of Glycopeptide Antibiotics. In: Lebl, M., Houghten, R.A. (eds) Peptides: The Wave of the Future. American Peptide Symposia, vol 7. Springer, Dordrecht. https://doi.org/10.1007/978-94-010-0464-0_222
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DOI: https://doi.org/10.1007/978-94-010-0464-0_222
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