Open AccessCorrelation Between the Binding of β-Lactam Antibiotics to Staphylococcus aureus and Their Physical-Chemical Properties
Author(s) -
James A. Retsema,
Verne A. Ray
Publication year - 1972
Publication title -
antimicrobial agents and chemotherapy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.07
H-Index - 259
eISSN - 1070-6283
pISSN - 0066-4804
DOI - 10.1128/aac.2.3.173
Subject(s) - staphylococcus aureus , benzylpenicillin , penicillin , antibiotics , lactam , chemistry , cephalosporin , microbiology and biotechnology , penicillin binding proteins , cell wall , bacteria , biochemistry , biology , stereochemistry , genetics
The rate of14 C-benzylpenicillin (penicillin G) binding toStaphylococcus aureus Oxford cells increased with increasing hydrogen ion concentration. The extent of inhibition of14 C-penicillin G binding caused by a competing12 C-β-lactam antibiotic is a function of hydrogen ion concentration and can be correlated both with net charge of a competing12 C-molecule and net charge of theS. aureus cell at a givenp H. The ability of a β-lactam antibiotic to compete for14 C-penicillin G-binding sites can generally be correlated with its hydrophobic nature. It is proposed that, although semisynthetic cephalosporins are chemically less reactive than penicillins, they are superior to benzylpenicillin in their ability to permeate the outer surface of theStaphylococcus cell wall and irreversibly bind to reactive sites.