ArticleScientific reports2019
High-resolution experimental and computational electrophysiology reveals weak β-lactam binding events in the porin PorB.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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Who cites it
5 citing papers in PubMed, 14 citations in OpenAlex.
- Probing Voltage Dependence Interaction of Cationic Peptides with Bacterial Porins at A Single-Molecule Level.Cell biochemistry and biophysics · 2026Article
- Genomic and Transcriptomic Analyses Reveal Multiple Strategies forFoods (Basel, Switzerland) · 2024Article
- An antibiotic-resistance conferring mutation in a neisserial porin: Structure, ion flux, and ampicillin binding.Biochimica et biophysica acta. Biomembranes · 2021Article
- Analysis of patchclamp recordings: model-free multiscale methods and software.European biophysics journal : EBJ · 2021Article
- Permeation of β-Lactamase Inhibitors through the General Porins of Gram-Negative Bacteria.Molecules (Basel, Switzerland) · 2020Article
Corrections and comments
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Authors and funding
10 authors at 5 institutions in 3 countries.
Funding
Abstract
The permeation of most antibiotics through the outer membrane of Gram-negative bacteria occurs through porin channels. To design drugs with increased activity against Gram-negative bacteria in the face of the antibiotic resistance crisis, the strict constraints on the physicochemical properties of the permeants imposed by these channels must be better understood. Here we show that a combination of high-resolution electrophysiology, new noise-filtering analysis protocols and atomistic biomolecular simulations reveals weak binding events between the β-lactam antibiotic ampicillin and the porin PorB from the pathogenic bacterium Neisseria meningitidis. In particular, an asymmetry often seen in the electrophysiological characteristics of ligand-bound channels is utilised to characterise the binding site and molecular interactions in detail, based on the principles of electro-osmotic flow through the channel. Our results provide a rationale for the determinants that govern the binding and permeation of zwitterionic antibiotics in porin channels.
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Registered trials
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