Native globular ferritin nanopore sensor

Yun-Dong Yin, Yu-Wei Zhang, Xi-Tong Song, Jun Hu, Yu-Heng Chen, Wen-Chuan Lai, Ya-Fei Li and Zhi-Yuan Gu ()
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Yun-Dong Yin: Nanjing Normal University
Yu-Wei Zhang: Nanjing Normal University
Xi-Tong Song: Nanjing Normal University
Jun Hu: Nanjing Normal University
Yu-Heng Chen: Nanjing Normal University
Wen-Chuan Lai: Nanjing Normal University
Ya-Fei Li: Nanjing Normal University
Zhi-Yuan Gu: Nanjing Normal University

Nature Communications, 2025, vol. 16, issue 1, 1-12

Abstract: Abstract High-resolution nanopore analysis technology relies on the design of novel transmembrane protein platforms. Traditional barrel-shaped protein channels are preferred for constructing nanopore sensors, which may miss protein candidates in non-barrel structures. Here, we demonstrate the globular ferritin displays excellent membrane-insertion capacity and stable transmembrane ionic current owing to its hydrophobic four-fold channels and hydrophilic three-fold channels. The ionic current rectification and voltage-gating characteristics are discovered in single-ferritin ionic current measurement. Notably, the ferritin is used as a nanopore sensor, by which we achieve the high resolution discrimination of L-cysteine, L-homocysteine, and cysteine-containing dipeptides with the assistance of equivalent Cu2+. The mechanistic studies by multiple controlled experiments and quantum mechanics/all-atom/coarse-grained multiscale MD simulations reveal that analytes are synergistically captured by His114, Cys126, and Glu130 within C3 channel, causing the current blockage signals. The promising ferritin nanopore sensor provides a guide to discovering new protein nanopores without shape restrictions.

Date: 2025
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DOI: 10.1038/s41467-025-60322-2

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