Glycopeptide antibiotics
Glycopeptide Antibiotics
Glycopeptide antibiotics (pronunciation: gly·co·pep·tide an·ti·bi·ot·ics) are a class of antibiotic drugs that inhibit the synthesis of bacterial cell walls. The term "glycopeptide" is derived from the Greek words "glykos" meaning sweet and "peptos" meaning digested, referring to the sugar-peptide structure of these antibiotics.
History
Glycopeptide antibiotics were first discovered in the 1950s, with Vancomycin being the first to be isolated and characterized. Since then, several other glycopeptide antibiotics have been discovered, including Teicoplanin, Bleomycin, and Ramoplanin.
Mechanism of Action
Glycopeptide antibiotics work by binding to the D-Ala-D-Ala terminus of the cell wall precursor, preventing the addition of new units to the peptidoglycan chain. This inhibits the synthesis of the bacterial cell wall, leading to cell death.
Clinical Use
Glycopeptide antibiotics are used to treat serious, life-threatening infections caused by gram-positive bacteria, including MRSA, Enterococcus species, and Clostridium difficile. They are often used as a last resort when other antibiotics are ineffective.
Side Effects
Common side effects of glycopeptide antibiotics include kidney damage, hearing loss, and allergic reactions. Due to these potential side effects, they are typically reserved for severe or resistant infections.
Resistance
Resistance to glycopeptide antibiotics is a growing concern. The most common mechanism of resistance is the alteration of the D-Ala-D-Ala target site to D-Ala-D-Lac or D-Ala-D-Ser, which reduces the binding affinity of the antibiotic.
See Also
References
External links
- Medical encyclopedia article on Glycopeptide antibiotics
- Wikipedia's article - Glycopeptide antibiotics
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