LPZ-51

LPZ-51 inhibits purified recombinant VbrKCA domain protein with a K_i value of 1.09 μM^[1].
LPZ-51 (1, 10 μg/mL) suppresses blaA transcription in V. parahemolyticus, achieving 77% inhibition at 1 μg/mL^[1].
LPZ-51 (0.5-50 μg/mL) dose-dependently reduces β-lactamase activity in V. parahemolyticus^[1].
LPZ-51 directly engages VbrK in V. parahemolyticus cells, increasing VbrK thermal stability by a ΔT_m of 4.1 °C^[1].
LPZ-51 (up to 128 μg/mL) synergizes with a broad range of β-lactam antibiotics (penicillins, cephalosporins, monobactam) against β-lactam-resistant V. parahemolyticus O3:K6 strain RIMD 2210633, with no effect on vancomycin resistance^[1].
LPZ-51 (up to 64 μg/mL) strongly synergizes with Carbenicillin against both SBL-producing and MBL-producing/carbapenem-resistant β-lactam-resistant V. parahemolyticus isolates, with FICI values ≤ 0.05 and ≤ 0.03, respectively^[1].
LPZ-51 (2 μg/mL; 15 consecutive passages) imposes a higher barrier to resistance development in V. parahemolyticus^[1].
LPZ-51 (1-10 μM) shows preliminary selectivity against a panel of 80 human kinases, with >50% inhibition of 7 kinases at 10 μM and sustained inhibition of PIM1, GAK, and NEK1 at 1 μM^[1].
LPZ-51 (up to 100 μg/mL) minimally inhibits HaCaT human keratinocyte cell viability^[1].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.