Tuning Electrostatic Gating of Semiconducting Carbon Nanotubes by Controlling Protein Orientation in Biosensing Devices.

Biosensors antimicrobial resistance carbon nanotubes protein engineering protein orientation

Journal

Angewandte Chemie (Weinheim an der Bergstrasse, Germany)
ISSN: 0044-8249
Titre abrégé: Angew Chem Weinheim Bergstr Ger
Pays: Germany
ID NLM: 100955692

Informations de publication

Date de publication:
06 Sep 2021
Historique:
received: 22 03 2021
revised: 24 06 2021
medline: 6 9 2021
pubmed: 6 9 2021
entrez: 20 3 2024
Statut: ppublish

Résumé

The ability to detect proteins through gating conductance by their unique surface electrostatic signature holds great potential for improving biosensing sensitivity and precision. Two challenges are: (1) defining the electrostatic surface of the incoming ligand protein presented to the conductive surface; (2) bridging the Debye gap to generate a measurable response. Herein, we report the construction of nanoscale protein-based sensing devices designed to present proteins in defined orientations; this allowed us to control the local electrostatic surface presented within the Debye length, and thus modulate the conductance gating effect upon binding incoming protein targets. Using a β-lactamase binding protein (BLIP2) as the capture protein attached to carbon nanotube field effect transistors in different defined orientations. Device conductance had influence on binding TEM-1, an important β-lactamase involved in antimicrobial resistance (AMR). Conductance increased or decreased depending on TEM-1 presenting either negative or positive local charge patches, demonstrating that local electrostatic properties, as opposed to protein net charge, act as the key driving force for electrostatic gating. This, in turn can, improve our ability to tune the gating of electrical biosensors toward optimized detection, including for AMR as outlined herein. Nanoscale protein‐based sensing devices designed to present proteins in defined orientations allowed the control of local electrostatic surface presented within the Debye length, and thus modulation of the conductance gating effect upon sensing protein targets.

Autres résumés

Type: Publisher (ger)
Nanoscale protein‐based sensing devices designed to present proteins in defined orientations allowed the control of local electrostatic surface presented within the Debye length, and thus modulation of the conductance gating effect upon sensing protein targets.

Identifiants

pubmed: 38504924
doi: 10.1002/ange.202104044
pii: ANGE202104044
pmc: PMC10946871
doi:

Types de publication

Journal Article

Langues

eng

Pagination

20346-20351

Informations de copyright

© 2021 The Authors. Angewandte Chemie published by Wiley-VCH GmbH.

Déclaration de conflit d'intérêts

The authors declare no conflict of interest.

Auteurs

Xinzhao Xu (X)

Department of Chemistry and Materials Research Institute Queen Mary University of London London E1 4NS UK.

Benjamin J Bowen (BJ)

Molecular Biosciences Division School of Biosciences Sir Martin Evans Building Cardiff University Cardiff CF10 3AX UK.

Rebecca E A Gwyther (REA)

Molecular Biosciences Division School of Biosciences Sir Martin Evans Building Cardiff University Cardiff CF10 3AX UK.

Mark Freeley (M)

Department of Chemistry and Materials Research Institute Queen Mary University of London London E1 4NS UK.

Bella Grigorenko (B)

Department of Chemistry Lomonosov Moscow State University Moscow 119991 Russian Federation.
Emanuel Institute of Biochemical Physics Russian Academy of Sciences Moscow 119991 Russian Federation.

Alexander V Nemukhin (AV)

Department of Chemistry Lomonosov Moscow State University Moscow 119991 Russian Federation.
Emanuel Institute of Biochemical Physics Russian Academy of Sciences Moscow 119991 Russian Federation.

Johnas Eklöf-Österberg (J)

Department of Chemistry and Chemical Engineering Chalmers University of Technology 41296 Gothenburg Sweden.

Kasper Moth-Poulsen (K)

Department of Chemistry and Chemical Engineering Chalmers University of Technology 41296 Gothenburg Sweden.

D Dafydd Jones (DD)

Molecular Biosciences Division School of Biosciences Sir Martin Evans Building Cardiff University Cardiff CF10 3AX UK.

Matteo Palma (M)

Department of Chemistry and Materials Research Institute Queen Mary University of London London E1 4NS UK.

Classifications MeSH