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. 1972 Sep;2(3):173–180. doi: 10.1128/aac.2.3.173

Correlation Between the Binding of β-Lactam Antibiotics to Staphylococcus aureus and Their Physical-Chemical Properties

James A Retsema 1, Verne A Ray 1
PMCID: PMC444286  PMID: 4790555

Abstract

The rate of 14C-benzylpenicillin (penicillin G) binding to Staphylococcus aureus Oxford cells increased with increasing hydrogen ion concentration. The extent of inhibition of 14C-penicillin G binding caused by a competing 12C-β-lactam antibiotic is a function of hydrogen ion concentration and can be correlated both with net charge of a competing 12C-molecule and net charge of the S. aureus cell at a given pH. The ability of a β-lactam antibiotic to compete for 14C-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 the Staphylococcus cell wall and irreversibly bind to reactive sites.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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