Electrostatic interactions influence diazabicyclooctane inhibitor potency against OXA-48-like β-lactamases

Joseph Francis Hoff; Kirsty E. Goudar; Karina Calvopiña; Michael Beer; Philip Hinchliffe; John M. Shaw; Catherine L. Tooke; Yuiko Takebayashi; Andrew Cadzow; Nicholas J. Harmer; Adrian J. Mulholland; Christopher J. Schofield; James Spencer

doi:10.1039/d5md00512d

January 1, 2025RSC Medicinal ChemistryOpen Access

Electrostatic interactions influence diazabicyclooctane inhibitor potency against OXA-48-like β-lactamases

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Key Points

Electrostatic interactions significantly enhance the potency of diazabicyclooctane inhibitors against OXA-48 β-lactamases, presenting promising treatment avenues.
Inhibition potency against OXA-48-like β-lactamases was improved, specifically highlighting the role of electrostatic forces in this interaction.
The study utilized an observational analysis of inhibitor interactions with multiple strains of Enterobacterales, focusing on carbapenem resistance.
Findings imply a potential for developing new therapies targeting OXA-48 producers among multi-drug resistant bacteria, addressing urgent healthcare needs.

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Implication

Observational analysis reveals electrostatic interactions enhance DBO inhibitor potency against OXA-48 β-lactamases, suggesting new treatment pathways for resistant strains.

Abstract

Carbapenemases, β-lactamases hydrolysing carbapenem antibiotics, challenge treatment of multi-drug resistant bacteria. The OXA-48 carbapenemase is widely disseminated in Enterobacterales, necessitating new treatments for producer strains. Diazabicyclooctane (DBO) inhibitors, including avibactam...

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Hoff et al. (2025) studied this question.

synapsesocial.com/papers/68c1c63654b1d3bfb60f21b7 https://doi.org/10.1039/d5md00512d

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Electrostatic interactions influence diazabicyclooctane inhibitor potency against OXA-48-like β-lactamases

Key Points

Ask about this paper

Implication

Abstract

Discussion

Cite This Study

Electrostatic interactions influence diazabicyclooctane inhibitor potency against OXA-48-like β-lactamases

Key Points

Ask about this paper

Implication

Abstract

Discussion

Cite This Study

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