Sequencing of proteins is a technically difficult task that typically requires digestion into short peptides before detection and identification. We developed a digestion-free method to chemically unfold and ‘scan’ full-length proteins through a nanopore, producing electrical fingerprints unique to individual protein molecules that are useful in their identification.
This is a preview of subscription content, log in via an institution to check access.
References
Alfaro, J. A. et al. The emerging landscape of single-molecule protein sequencing technologies. Nat. Methods 18, 604–617 (2021). This review article presents the development of protein sequencing technologies.
Deamer, D., Akeson, M. & Branton, D. Three decades of nanopore sequencing. Nat. Biotechnol. 34, 518–524 (2016). This review article summarizes three decades of nanopore sequencing.
Yu, L. et al. Stable polymer bilayers for protein channel recordings at high guanidinium chloride concentrations. Biophys. J. 120, 1537–1541 (2021). This paper reports a suitable polymer bilayer for denatured protein sensing using a biological nanopore.
Kang, X., Alibakhshi, M. A. & Wanunu, M. One-pot species release and nanopore detection in a voltage-stable lipid bilayer platform. Nano Lett 19, 9145–9153 (2019). This paper reports a wedge-on-pillar membrane support for nanopore experiments.
Additional information
Publisher’s note Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.
This is a summary of: Yu, L. et al. Unidirectional single-file transport of full-length proteins through a nanopore. Nat. Biotechnol. https://doi.org/10.1038/s41587-022-01598-3 (2023)
Rights and permissions
About this article
Cite this article
Protein identification using a digestion-free nanopore approach. Nat Biotechnol 41, 1078–1079 (2023). https://doi.org/10.1038/s41587-022-01599-2
Published:
Issue Date:
DOI: https://doi.org/10.1038/s41587-022-01599-2
- Springer Nature America, Inc.