Glycopeptides
Information about Glycopeptides[edit source]
The glycopeptide antibiotics are semisynthetic macromolecules that are structurally related to vancomycin and have antibacterial activity against several gram positive organisms including methicillin resistant Staphylococcus aureus (MRSA).
List of Glycopeptides[edit source]
Three lipoglycopeptide antibiotics are available for use in the United States: dalbavancin, oritavancin and telavancin. All three agents have been associated with transient serum enzyme elevations during therapy, but they have yet to be linked convincingly to cases of clinically apparent acute liver injury.
Mechanism of action of Glycopeptides[edit source]
The glycopeptide antibiotics are a class of antimicrobial agents that share a similar, macromolecular structure and basic mechanism of action. The lipoglycopeptides are largely synthetic derivatives of vancomycin modified to have greater potency or better pharmacokinetics and tolerance. Like vancomycin, these agents have potent antibacterial activity against several Streptococcus and Enterococcus species as well as Staphylococcus aureus, including strains that are methicillin-resistant (MRSA). The agents are macromolecular glycopeptides that act by binding to nascent bacterial cell wall peptidoglycans, thus interfering with cell wall synthesis. The lipoglycopeptides are not absorbed orally and have a prolonged half-life when given intravenously which allows for once daily and, in some cases, once weekly administration. Vancomycin is a similar glycopeptide, but its indications, wide scale use and record of safety are greater than the more recently approved lipoglycopeptide derivatives.
FDA approval information for Glycopeptides[edit source]
Three lipoglycopeptide antibiotics have been approved for use in the United States and are discussed together: telavancin (2009), dalbavancin (2014) and oritavancin (2014).
List of Glycopeptides[edit source]
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