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Chemistry and biology of the ramoplanin family of peptide antibiotics.

Publication ,  Journal Article
McCafferty, DG; Cudic, P; Frankel, BA; Barkallah, S; Kruger, RG; Li, W
Published in: Biopolymers
January 2002

The peptide antibiotic ramoplanin factor A2 is a promising clinical candidate for treatment of Gram-positive bacterial infections that are resistant to antibiotics such as glycopeptides, macrolides, and penicillins. Since its discovery in 1984, no clinical or laboratory-generated resistance to this antibiotic has been reported. The mechanism of action of ramoplanin involves sequestration of peptidoglycan biosynthesis Lipid intermediates, thus physically occluding these substrates from proper utilization by the late-stage peptidoglycan biosynthesis enzymes MurG and the transglycosylases (TGases). Ramoplanin is structurally related to two cell wall active lipodepsipeptide antibiotics, janiemycin, and enduracidin, and is functionally related to members of the lantibiotic class of antimicrobial peptides (mersacidin, actagardine, nisin, and epidermin) and glycopeptide antibiotics (vancomycin and teicoplanin). Peptidomimetic chemotherapeutics derived from the ramoplanin sequence may find future use as antibiotics against vancomycin-resistant Enterococcus faecium (VRE), methicillin-resistant Staphylococcus aureus (MRSA), and related pathogens. Here we review the chemistry and biology of the ramoplanins including its discovery, structure elucidation, biosynthesis, antimicrobial activity, mechanism of action, and total synthesis.

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Published In

Biopolymers

DOI

EISSN

1097-0282

ISSN

0006-3525

Publication Date

January 2002

Volume

66

Issue

4

Start / End Page

261 / 284

Related Subject Headings

  • Protein Conformation
  • Peptides, Cyclic
  • Molecular Sequence Data
  • Models, Molecular
  • Gram-Positive Bacterial Infections
  • Depsipeptides
  • Biophysics
  • Bacteria
  • Anti-Bacterial Agents
  • Amino Acid Sequence
 

Citation

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McCafferty, D. G., Cudic, P., Frankel, B. A., Barkallah, S., Kruger, R. G., & Li, W. (2002). Chemistry and biology of the ramoplanin family of peptide antibiotics. Biopolymers, 66(4), 261–284. https://doi.org/10.1002/bip.10296
McCafferty, Dewey G., Predrag Cudic, Brenda A. Frankel, Salim Barkallah, Ryan G. Kruger, and Wenkai Li. “Chemistry and biology of the ramoplanin family of peptide antibiotics.Biopolymers 66, no. 4 (January 2002): 261–84. https://doi.org/10.1002/bip.10296.
McCafferty DG, Cudic P, Frankel BA, Barkallah S, Kruger RG, Li W. Chemistry and biology of the ramoplanin family of peptide antibiotics. Biopolymers. 2002 Jan;66(4):261–84.
McCafferty, Dewey G., et al. “Chemistry and biology of the ramoplanin family of peptide antibiotics.Biopolymers, vol. 66, no. 4, Jan. 2002, pp. 261–84. Epmc, doi:10.1002/bip.10296.
McCafferty DG, Cudic P, Frankel BA, Barkallah S, Kruger RG, Li W. Chemistry and biology of the ramoplanin family of peptide antibiotics. Biopolymers. 2002 Jan;66(4):261–284.
Journal cover image

Published In

Biopolymers

DOI

EISSN

1097-0282

ISSN

0006-3525

Publication Date

January 2002

Volume

66

Issue

4

Start / End Page

261 / 284

Related Subject Headings

  • Protein Conformation
  • Peptides, Cyclic
  • Molecular Sequence Data
  • Models, Molecular
  • Gram-Positive Bacterial Infections
  • Depsipeptides
  • Biophysics
  • Bacteria
  • Anti-Bacterial Agents
  • Amino Acid Sequence