Abstract
Glycopeptide antibiotics (GPAs) are an important class of secondary metabolites produced by various actinobacteria, with the most prominent members being vancomycin and teicoplanin. The heptapeptide backbone of GPAs is assembled by a nonribosomal peptide synthetase (NRPS), with subsequent oxidative crosslinking leading to a highly rigid compound that can interfere with bacterial cell wall maturation through binding to the precursor lipid II. GPAs contain a range of unusual amino acid precursors and an extensive suite of modifications that are installed during and after peptide assembly, which includes chlorination, hydroxylation, glycosylation, acylation, sulfation, and methylation. In this article, we discuss the structures of different GPAs, their biosynthetic gene clusters and biosynthesis, the effects of various tailoring steps on their bioactivity, as well as the emerging resistance of pathogenic bacteria and possibilities to overcome such resistance through GPA redesign.
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