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Cited by 3Antibiotic Resistance in BacteriaSynthesis of β-Lactam CompoundsEnzyme function and inhibition

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

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Hoff, Joseph F., Goudar, Kirsty E., Calvopiña, Karina, Beer, Michael, Hinchliffe, Philip, Shaw, John M., Tooke, Catherine L., Takebayashi, Yuiko, Cadzow, Andrew F., Harmer, Nicholas J., Mulholland, Adrian J., Schofield, Christopher J., Spencer, James·2025·RSC Medicinal Chemistry
DOI 10.1039/d5md00512dPMC PMC12415477

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Abstract

The OXA-48 β-lactamase protects bacteria from carbapenem antibiotics; with activity affected by sequence variation. We show variation to affect susceptibility towards diazabicyclooctane (DBO) inhibitors, dependent upon the inhibitor C2 substituent.

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Metadata

Authors
Hoff, J. F., Goudar, K. E., Calvopiña, K., Beer, M., Hinchliffe, P., Shaw, J. M., Tooke, C. L., Takebayashi, Y., Cadzow, A. F., Harmer, N. J., Mulholland, A. J., Schofield, C. J., & Spencer, J.
Affiliations
  • University of Bristol (GB)
  • University of Oxford (GB)
  • University of Exeter (GB)
Corresponding author
Spencer, James
ORCID
Venue
RSC Medicinal Chemistry
Publisher
Royal Society of Chemistry (RSC)
Published
2025
Volume
16
Issue
11
Pages
5441-5455
ISSN
2632-8682 (ISSN-L)
DOI
10.1039/d5md00512d
PMC
PMC12415477
OpenAlex
W4413253057
Cited by
3
References
1
Citations by year
2026: 3
FWCI
0.84
Type
journal article
Language
en
Open access
Licence
Locations
  • RSC Medicinal Chemistry (publishedVersion, cc-by)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
  • PubMed (publishedVersion)
  • PubMed Central (publishedVersion, cc-by)
  • Explore Bristol Research (publishedVersion, cc-by)
  • Bristol Research (University of Bristol) (publishedVersion, cc-by)
  • Bristol Research (University of Bristol) (submittedVersion, cc-by-nc-nd)
Funders
  • Medical Research Council (MR/T016035/1, MR/W006308/1)
  • Biotechnology and Biological Sciences Research Council (BB/T008741/1, BB/W001187/1)
  • H2020 European Research Council (PREDACTED Advanced Grant Agreement no. 101021207)
Topics
  • Health Sciences › Medicine › Microbiology (medical) › Antibiotic Resistance in Bacteria
  • Physical Sciences › Chemistry › Organic Chemistry › Synthesis of β-Lactam Compounds
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Enzyme function and inhibition
Keywords
avibactam, OXA-48, metallo-beta-lactamase, electrostatic interactions, inhibitor potency, desulfation, carbapenem resistance, molecular dynamics simulation, crystal structure

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