In Vitro | Vaborbactam (RPX-7009; MP-7009) is a broad spectrum of inhibition of β-lactamases, with particularly potent activity against KPC, CTX-M, SHV, and CMY enzymes[1]. Vaborbactam restores meropenem activity for 72.7 to 98.1% of CPE isolates at ≤2 μg/mL, and maximum potentiation is achieved with fixed concentrations of ≥8 μg/mL of the inhibitor (≥96.5% of isolates are inhibited at ≤2 μg/mL of meropenem-vaborbactam). Meropenem-vaborbactam with a fixed concentration of 8 μg/mL of the inhibitor (MIC50, ≤0.06 μg/mL for all organisms) inhibits 93.7% of the CPE isolates displaying elevated meropenem MICs at ≤1 μg/mL[2]. By forming a reversible dative bond with the blactamase, vaborbactam acts as a competitive inhibitor and is not hydrolyzed by the b-lactamase[3]. |
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