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Exploring New Nanopore Sensors from the Aerolysin Family
Juan F Bada Juarez1, Nuria Cirauqui1, Fernando Augusto T P Meireles1
1Institute of Bioengineering, School of Life Sciences, EPFL, Lausanne, 1015, Switzerland.
Small (Weinheim an Der Bergstrasse, Germany)
|July 8, 2025
Summary
Aerolysin-like proteins show promise as nanopore sensors. Clostridium perfringens epsilon toxin (ETX) demonstrated enhanced sensitivity for single-strand DNA (ssDNA) sensing compared to aerolysin.
Area of Science:
- Biochemistry
- Biophysics
- Nanotechnology
Background:
- Aerolysin-like proteins are pore-forming toxins with potential in nanopore sensing.
- Low sequence identity among these proteins hinders understanding of their pore structure and properties.
Purpose of the Study:
- To analyze and compare the pore structures of ETX, LSL, and Bacillus thuringiensis parasporin-2.
- To assess their single-strand DNA (ssDNA) sensing capabilities.
- To experimentally characterize ETX pore conformations and ssDNA translocation.
Main Methods:
- In silico analysis of aerolysin-like protein structures.
- Computational assessment of ssDNA sensing.
- Experimental characterization of Clostridium perfringens epsilon toxin (ETX) pore conformations and ssDNA translocation.
Main Results:
- Three distinct pore conformations of ETX were identified, each with unique current properties.
- Only one ETX pore conformation translocated ssDNA.
- ETX showed greater current blockage depth than aerolysin during ssDNA translocation, indicating higher sensitivity.
Conclusions:
- Aerolysin-like proteins offer diverse nanopore sensing capabilities.
- ETX exhibits superior ssDNA sensing sensitivity, paving the way for improved molecular detection.
- Findings support the development of novel nanopore sensors for biomolecular applications.
