@article{bada_juarez_exploring_2025, title = {Exploring New Nanopore Sensors from the Aerolysin Family}, issn = {1613-6810, 1613-6829}, url = {https://onlinelibrary.wiley.com/doi/10.1002/smll.202501219}, doi = {10.1002/smll.202501219}, abstract = {Abstract Aerolysin‐like proteins are a family of pore‐forming toxins with potential biotechnological applications as nanopore sensors for biomolecular detection and sequencing. Despite their conserved structural fold, the low sequence identity complicates sequence alignment, limiting the understanding of their pore structure and properties. Here, the pore structures of three family members – Clostridium perfringens epsilon toxin ({ETX}), Laetiporus sulphureus lectin ({LSL}), and Bacillus thuringiensis parasporin‐2 – are analyzed and compared to aerolysin and assess their single‐strand {DNA} ({ssDNA}) sensing capabilities through in silico methods. {ETX} is further characterized experimentally, revealing three distinct pore conformations, each with specific open pore currents, only one of which translocates {ssDNA}. Notably, {ETX} exhibited higher current blockage depth compared to aerolysin during {ssDNA} translocation, indicating a higher sensitivity for molecular sensing. The findings open new avenues for improving and diversifying nanopore capabilities in molecular sensing.}, pages = {2501219}, journaltitle = {Small}, shortjournal = {Small}, author = {Bada Juarez, Juan F. and Cirauqui, Nuria and Meireles, Fernando Augusto T. P. and Perrin, Louis W. and Barry, Julian and Bokori‐Brown, Monika and Marcaida, Maria J. and Cao, Chan and Dal Peraro, Matteo}, urldate = {2025-07-16}, date = {2025-07-07}, langid = {english}, }