Glycopeptide antibiotic

Glycopeptide antibiotics are a class of drugs of microbial origin that are composed of glycosylated cyclic or polycyclic nonribosomal peptides. Significant glycopeptide antibiotics include the anti-infective antibiotics vancomycin, teicoplanin, telavancin, ramoplanin and decaplanin, and the antitumor antibiotic bleomycin. Vancomycin is used if infection with methicillin-resistant Staphylococcus aureus (MRSA) is suspected.

Some members of this class of drugs inhibit the synthesis of cell walls in susceptible microbes by inhibiting peptidoglycan synthesis. They bind to the amino acids within the cell wall preventing the addition of new units to the peptidoglycan. In particular, they bind to acyl-D-alanyl-D-alanine in peptidoglycan.

Due to their toxicity, use of glycopeptide antibiotics is restricted to patients who are critically ill, who have a demonstrated hypersensitivity to the β-lactams, or who are infected with β-lactam-resistant species. These antibiotics are effective principally against Gram-positive cocci. They exhibit a narrow spectrum of action, and are bactericidal only against the enterococci. Some tissues are not penetrated very well by glycopeptides, and they do not penetrate into the cerebrospinal fluid.

Vancomycin was isolated in 1953, and used clinically from 1955. Approved in 1958 by FDA to treat penicillin resistant staphylococci. MRSA first seen in 1961. Bleomycin was first discovered in 1966. Teicoplanin was discovered in the early 1990s. Telavancin is a semi-synthetic lipoglycopeptide derivative of vancomycin (approved by FDA in 2009).

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