Glycopeptide antibiotic

Glycopeptide antibiotics (pronunciation: gly·co·pep·tide an·ti·bi·ot·ics) are a class of antibiotics that inhibit the synthesis of bacterial cell walls. The term "glycopeptide" is derived from the Greek words "glykos" meaning sweet and "peptos" meaning cooked or digested, referring to the sugar-peptide structure of these antibiotics.

History

Glycopeptide antibiotics were first discovered in the 1950s, with Vancomycin being the first member of this class to be identified. Since then, several other glycopeptide antibiotics such as Teicoplanin and Telavancin have been discovered and used in clinical practice.

Mechanism of Action

Glycopeptide antibiotics work by binding to the D-alanyl-D-alanine terminus of the cell wall precursor, preventing the addition of new units to the peptidoglycan chain. This results in a weakened cell wall and eventually leads to cell lysis and death.

Clinical Use

Glycopeptide antibiotics are primarily used to treat serious, life-threatening infections caused by gram-positive bacteria, including Methicillin-resistant Staphylococcus aureus (MRSA) and Enterococcus species. They are often used as a last resort when other antibiotics are ineffective.

Resistance

Resistance to glycopeptide antibiotics is a growing concern in the medical community. The most common mechanism of resistance involves the alteration of the D-alanyl-D-alanine target site to D-alanyl-D-lactate or D-alanyl-D-serine, which reduces the binding affinity of the antibiotic.