Differential inhibition of Staphylococcus aureus PBP2 by glycopeptide antibiotics.
J Am Chem Soc
; 127(10): 3250-1, 2005 Mar 16.
Article
em En
| MEDLINE
| ID: mdl-15755121
ABSTRACT
The glycopeptide antibiotics prevent maturation of the bacterial cell wall by binding to the terminal d-alanyl-d-alanine moiety of peptidoglycan precursors, thereby inhibiting the enzymes involved in the final stages of peptidoglycan synthesis. However, there are significant differences in the biological activity of particular glycopeptide derivatives that are not related to their affinity for d-Ala-d-Ala. We compare the ability of vancomycin and a set of clinically relevant glycopeptides to inhibit Staphylococcus aureus PBP2 (penicillin binding protein), the major transglycosylase in a clinically relevant pathogen, S. aureus. We report experiments suggesting that activity differences between glycopeptides against this organism reflect a combination of substrate binding and secondary interactions with key enzymes involved in peptidoglycan synthesis.
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Base de dados:
MEDLINE
Assunto principal:
Staphylococcus aureus
/
Uridina Difosfato Ácido N-Acetilmurâmico
/
Vancomicina
/
Proteínas de Ligação às Penicilinas
/
Antibacterianos
Idioma:
En
Ano de publicação:
2005
Tipo de documento:
Article