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• W2133919851 abstract "Abstract The functional definition of extended‐spectrum β ‐lactamase (ESBL) activity is a clinical challenge. Here we report a rapid and convenient assay of β ‐lactamase activity through the competitive inhibition of fluorescent substrate hydrolysis that provides a read‐out nearly 40× more rapidly than conventional techniques for functional definition. A panel of β ‐lactam antibiotics was used for competition against β ‐lactamase enzyme‐activated photosensitizer ( β ‐LEAP) yielding a competitive index ( C i ) in 30 min. Significant differences in the relative C i values of the panel of β ‐lactams were determined in vitro for Bacillus cereus penicillinase. Additionally, the relative C i values for whole bacterial cell suspensions of B. cereus 5/ β were compared with the relative minimal inhibitory concentration (MIC) values and a correlation coefficient of 0.899 was determined. We further demonstrated the ability of β ‐LEAP to probe the capacity of ceftazidime to inhibit the enzyme activity of a panel of ESBL‐producing Escherichia coli . The bacteria were assayed for susceptibility to ceftazidime and the relative MIC values were compared with the relative C i values for ceftazidime yielding a correlation coefficient of 0.984. This work demonstrates for the first time the whole cell assay of the competitive inhibition of β ‐lactamase enzyme activity and derivation of associated constants." @default.
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• W2133919851 date "2010-09-20" @default.
• W2133919851 modified "2023-10-16" @default.
• W2133919851 title "Rapid Functional Definition of Extended Spectrum β-Lactamase Activity in Bacterial Cultures via Competitive Inhibition of Fluorescent Substrate Cleavage" @default.
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• W2133919851 doi "https://doi.org/10.1111/j.1751-1097.2010.00801.x" @default.
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