Methicillin-resistant Staphylococcus aureus (MRSA) and other multidrug-resistant strains of Gram-positive bacteria are particularly susceptible to the action of glycopeptide antibiotics. The glycosylated peptide structure that characterizes the chemical makeup of these antibiotics gives rise to their name. Two well-known members of the glycopeptide antibiotic family include vancomycin and teicoplanin. The
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Methicillin-resistant Staphylococcus aureus (MRSA) and other multidrug-resistant strains of Gram-positive bacteria are particularly susceptible to the action of glycopeptide antibiotics. The glycosylated peptide structure that characterizes the chemical makeup of these antibiotics gives rise to their name. Two well-known members of the glycopeptide antibiotic family include vancomycin and teicoplanin. The bacteria Streptomyces orientalis produced vancomycin, the first glycopeptide ever found, in 1953. As a potent antibiotic, it became widely utilized, particularly to treat serious infections brought on by Gram-positive bacteria that are resistant to other antibiotics. Similar modes of action are shared by tecoplanin, a semi-synthetic derivative of vancomycin that was produced subsequently. Glycopeptide antibiotics work primarily by preventing the formation of bacterial cell walls. Peptidoglycan is a complex substance that offers protection and structural support and makes up the cell walls of bacteria. By attaching to the expanding peptidoglycan chain's terminal D-alanine-D-alanine residues, glycopeptide antibiotics obstruct the formation of peptidoglycan. By blocking the transpeptidation process, this interaction eventually disrupts the cell wall by preventing the peptidoglycan strands from cross-linking.Over time, resistance to antibiotics containing glycopeptides has developed. One well-known method is the bacteria's modification of the target site, which lowers the antibiotics' binding affinity. Both Enterococcus faecalis and Enterococcus faecium strains have shown signs of this.Furthermore, the VanA gene cluster—which in certain bacteria codes for resistance—is transferable, which promotes the transmission of resistance genes between strains. Glycopeptide antibiotics are still essential for treating serious infections brought on by Gram-positive bacteria, even in the face of resistance. Because of their low oral absorption, they are usually administered intravenously and saved for cases where other antibiotics have failed. The goal of ongoing research is to find novel formulations and derivatives that solve resistance issues and guarantee the sustained effectiveness of glycopeptide antibiotics against emerging bacterial threats.
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