Structure, biochemistry and mechanism of action of glycopeptide antibiotics

@article{Reynolds2005StructureBA,
  title={Structure, biochemistry and mechanism of action of glycopeptide antibiotics},
  author={Peter E. Reynolds},
  journal={European Journal of Clinical Microbiology and Infectious Diseases},
  year={2005},
  volume={8},
  pages={943-950}
}
  • P. Reynolds
  • Published 1 November 1989
  • Biology, Chemistry
  • European Journal of Clinical Microbiology and Infectious Diseases
Glycopeptide antibiotics, including vancomycin and teicoplanin, are large, rigid molecules that inhibit a late stage in bacterial cell wall peptidoglycan synthesis. The three-dimensional structure contains a cleft into which peptides of highly specific configuration (L-aa-D-aa-D-aa) can fit: such sequences are found only in bacterial cell walls, hence glycopeptides are selectively toxic. Glycopeptides interact with peptides of this conformation by hydrogen bonding, forming stable complexes. As… 

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Mannopeptimycins, a novel class of glycopeptide antibiotics active against gram-positive bacteria

  • Hai-yin He
  • Biology, Chemistry
    Applied Microbiology and Biotechnology
  • 2004
The SAR data of the natural and synthetic esters demonstrate that the presence of hydrophobic groups near the terminal mannosyl moiety is critical for antibacterial potency, and suggest that the mannopeptimycins interfere with the late stages of bacterial cell wall biosynthesis.

Structure determination of peptides with antimicrobial action

Peptide antibiotics belonging to three different families were investigated using X-ray crystallography. The peptaibol antibiotics cephaibol A, B and C gave well-diffracting crystals and their
...

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