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ß-Lactamase-Inhibitor Protein Binding Affinities: Detection of Hydrolysis of ß-Lactam Substrate by TEM-1 Enzyme and Inhibitor Binding Using The FlexStation® 3 Microplate Reader
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Molecular Devices

Bacterial resistance to ß-lactam drugs through the production of class A ß-lactamase enzymes is an increasing concern in the medical community.1 ß-lactamase inhibitory protein (BLIP) produced by the soil bacterium Streptomyces clavuligeris inhibits a number of class A ß-lactamases with a wide range of affinities, thereby restoring the effectiveness of life-saving antibiotics.2 BLIP’s known binding partners include Escherichia coli TEM-1, Serratia marcescens SME-1, Bacillus anthracis BlaI (nanomolar affinity for all three), Klebsiella pneumonia SHV-1 (micromolar affinity), and Proteus vulgaris K1 (picomolar affinity).(2-4) In spite of their ubiquity in biological systems, few rules governing the biochemical basis of affinity and specificity for protein interactions exist. What interactions are sufficient and necessary for successful inhibition? Insight into BLIP’s ability to recognize and inhibit a wide range of enzymes has immediate implications towards the development of novel therapeutics. Mutagenesis data is invaluable for gaining this insight.

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