Glycopeptide Antibiotics: Structure and Mechanisms of Action.
- Author:
Hee Kyoung KANG
1
;
Yoonkyung PARK
Author Information
- Publication Type:Review
- Keywords: Glycopeptide; Resistance; Vancomycin; Teicoplanin; Dalbavancin
- MeSH: Anti-Bacterial Agents*; Drug Resistance; Glycopeptides; Gram-Positive Bacteria; Gram-Positive Bacterial Infections; Humans; Incidence; Peptides; Teicoplanin; Vancomycin
- From:Journal of Bacteriology and Virology 2015;45(2):67-78
- CountryRepublic of Korea
- Language:English
- Abstract: Glycopeptides of the clinically important antibiotic drugs are glycosylated cyclic or polycyclic nonribosomal peptides. Glycopeptides such as vancomycin and teicoplanin are often used for the treatment of gram-positive bacteria in patients. The increased incidence of drug resistance and inadequacy of these therapeutics against gram-positive bacterial infections would be the formation and clinical development of more variable second generation of glycopeptide antibiotics: semisynthetic lipoglycopeptide analogs such as telavancin, dalbavancin, and oritavancin with improved activity and better pharmacokinetic properties. In this review, we describe the development of and bacterial resistance to vancomycin, teicoplanin, and semisynthetic glycopeptides (teicoplanin, dalbavancin, and oritavancin). The clinical influence of resistance to glycopeptides, particularly vancomycin, are also discussed.
