Evidence map›Paper›PMID 39209826›Full record

ArticleNature communications2024

Optimising CNT-FET biosensor design through modelling of biomolecular electrostatic gating and its application to β-lactamase detection.

Rebecca E A Gwyther, Sébastien Côté, Chang-Seuk Lee, Haosen Miao, Krithika Ramakrishnan, Matteo Palma, D Dafydd Jones

Abstract read
In one paragraph

Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

8 citing papers in PubMed.

  1. Article
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  5. Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors.

Rebecca E A Gwyther *Molecular Biosciences Division, School of Biosciences Cardiff University, Cardiff, UK.
Sébastien Côté *Département de Physique, Faculté des Arts et des Sciences, Université de Montréal, Montréal, QC, Canada. scote@cstj.qc.ca.ORCID 0000-0002-4672-7729
Chang-Seuk Lee *Department of Chemistry, Queen Mary University of London, London, UK.ORCID 0000-0002-5905-800X
Haosen MiaoDepartment of Chemistry, Queen Mary University of London, London, UK.
Krithika RamakrishnanMolecular Biosciences Division, School of Biosciences Cardiff University, Cardiff, UK.
Matteo PalmaDepartment of Chemistry, Queen Mary University of London, London, UK. m.palma@qmul.ac.uk.ORCID 0000-0001-8715-4034
D Dafydd JonesMolecular Biosciences Division, School of Biosciences Cardiff University, Cardiff, UK. jonesdd@cardiff.ac.uk.ORCID 0000-0001-7709-3995

Funding

RCUK | Biotechnology and Biological Sciences Research Council (BBSRC) BB/M009122/1RCUK | Engineering and Physical Sciences Research Council (EPSRC) EP/J015318/1RCUK | Engineering and Physical Sciences Research Council (EPSRC) EP/V048147/1Wellcome TrustWellcome Trust AC1910IF14
6 · The paper itself

Abstract

Carbon nanotube field effect transistors (CNT-FET) hold great promise as next generation miniaturised biosensors. One bottleneck is modelling how proteins, with their distinctive electrostatic surfaces, interact with the CNT-FET to modulate conductance. Using advanced sampling molecular dynamics combined with non-canonical amino acid chemistry, we model protein electrostatic potential imparted on single walled CNTs (SWCNTs). We focus on using β-lactamase binding protein (BLIP2) as the receptor as it binds the antibiotic degrading enzymes, β-lactamases (BLs). BLIP2 is attached via the single selected residue to SWCNTs using genetically encoded phenyl azide photochemistry. Our devices detect two different BLs, TEM-1 and KPC-2, with each BL generating distinct conductance profiles due to their differing surface electrostatic profiles. Changes in conductance match the model electrostatic profile sampled by the SWCNTs on BL binding. Thus, our modelling approach combined with residue-specific receptor attachment could provide a general approach for systematic CNT-FET biosensor construction.

Indexed as

beta-LactamasesBiosensing TechniquesMolecular Dynamics SimulationNanotubes, CarbonStatic ElectricityProtein BindingTransistors, Electronicbeta-LactamasesNanotubes, Carbon

Identifiers

PMID39209826
PMCPMC11362306

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.