The DOI matches its Crossref record; 43 of the 43 references it cites were found in a registry or an index.
Electrical recognition of the twenty proteinogenic amino acids using an aerolysin nanopore
Open accessAbstract
Efforts to sequence single protein molecules in nanopores1–5 have been hampered by the lack of techniques with sufficient sensitivity to discern the subtle molecular differences among all twenty amino acids. Here we report ionic current detection of all twenty proteinogenic amino acids in an aerolysin nanopore with the help of a short polycationic carrier. Application of molecular dynamics simulations revealed that the aerolysin nanopore has a built-in single-molecule trap that fully confines a polycationic carrier-bound amino acid inside the sensing region of the aerolysin. This structural feature means that each amino acid spends sufficient time in the pore for sensitive measurement of the excluded volume of the amino acid. We show that distinct current blockades in wild-type aerolysin can be used to identify 13 of the 20 natural amino acids. Furthermore, we show that chemical modifications, instrumentation advances and nanopore engineering offer a route toward identification of the remaining seven amino acids. These findings may pave the way to nanopore protein sequencing. Individual amino acids fused to a highly charged heptapeptide are discriminated in an aerolysin nanopore.
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Cites
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Cited by
The Human Proteoform Project: Defining the human proteome
Smith, L. M., Agar, J. N., Chamot-Rooke, J., Danis, P. O., Ge, Y., Loo, J. A., Paša-Tolić, L., Tsybin, Y. O., Kelleher, N. L., & The Consortium for Top-Down Proteomics (2021) · Science Advances · doi:10.1126/sciadv.abk0734 · Cited by 242
“Similarly, single-molecule MS (18–20), nanopore sequencing (21, 22), cryoelectron microscopy and visual proteomics (23, 24), single-cell proteomics (25–29), single-molecule protein arrays (30, 31), and other ideas yet to be conceived need to be encouraged, supported, and developed to advance proteoform biology.”
BackgroundAerolysin nanopores decode digital information stored in tailored macromolecular analytes
Cao, C., Krapp, L. F., Al Ouahabi, A., König, N. F., Cirauqui, N., Radenovic, A., Lutz, J.-F., & Peraro, M. D. (2020) · Science Advances · doi:10.1126/sciadv.abc2661 · Cited by 97
Mining folded proteomes in the era of accurate structure prediction
Bayly-Jones, C., & Whisstock, J. C. (2022) · PLOS Computational Biology · doi:10.1371/journal.pcbi.1009930 · Cited by 16
(2021) · doi:10.1016/j.isci.2021.103202 · Cited by 16
Peng, Z., Usami, M., Nakada, A., Sekiya, Y., Fujita, S., Mijiddorj, B., Kawamura, I., & Kawano, R. (2025) · ACS Nano · doi:10.1021/acsnano.5c15080 · Cited by 8
Metadata
- Authors
- Ouldali, H., Sarthak, K., Ensslen, T., Piguet, F., Manivet, P., Pelta, J., Behrends, J. C., Aksimentiev, A., & Oukhaled, A.
- Venue
- Nature Biotechnology
- Published
- 2019-12-16
- Volume
- 38
- Issue
- 2
- Pages
- 176-181
- ISSN
- 0733-222X (ISSN-L)
- 1087-0156
- 1546-1696
- OpenAlex
- W2995162887
- Cited by
- 474
- References
- 43
- FWCI
- 18.57
- Type
- journal article
- Language
- en
- Open access
- green
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