Glycopeptides
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, corbomycin, complestatin 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. Many
glycopeptides inhibit the function of glycosyltransferases, which polymerase amino acid/sugar building blocks into 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 by 1958, while teicoplanin was discovered in 1978 and became clinically-available in 1984. [1]. Telavancin is a semi-synthetic lipoglycopeptide derivative of
vancomycin approved by FDA in 2009.
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