Sandbox Reserved 992: Difference between revisions
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== Class C Inhibition == | == Class C Inhibition == | ||
With the mechanistic knowledge of β-lactamases, there are two apparent options for clinical treatment of β-lactam resistant bacteria. Scientists could either (a) design an entirely new class of antibiotic that are not reliant on the chemical structure of the β-lactam ring, or (b) use the current arsenal of antibiotics in combination with an inhibitor that will deactivate the β-lactamase. A β-lactamase inhibitor is a compound that could form a tight complex to the active site of the enzyme and causes the β-lactamase to be unable to bind and inactivate another antibiotic molecule. Links to examples Class C β-lactamases, both with and without clinical inhibitors bound, are provided. | With the mechanistic knowledge of β-lactamases, there are two apparent options for clinical treatment of β-lactam resistant bacteria. Scientists could either (a) design an entirely new class of antibiotic that are not reliant on the chemical structure of the β-lactam ring, or (b) use the current arsenal of antibiotics in combination with an inhibitor that will deactivate the β-lactamase. A β-lactamase inhibitor is a compound that could form a tight complex to the active site of the enzyme and causes the β-lactamase to be unable to bind and inactivate another antibiotic molecule. Links to examples Class C β-lactamases, both with and without clinical inhibitors bound, are provided.<ref>Powers, Rachel, Hollister C. Swanson, Magdalena A. Taracila, Nicholas W. Florek, Chiara Romagnoli, Emilia Caselli, Fabio Prati, Robert A. Bonomo, and Bradley J. Wallar. Biochemical and Structural Analysis of Inhibitors Targeting the ADC-7 Cephalosporinase of Acinetobacter baumannii. Biochemistry, 2014, 53 (48), 7670-7679.</ref> | ||
==References== | ==References== | ||
<references/> | <references/> | ||
