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SEQUENCING TECHNOLOGY

Reading amino acids in a nanopore

Nature Biotechnology volume 38, pages 159–160 (2020)Cite this article

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In a step toward nanopore sequencing of proteins, an aerolysin pore discriminates many of the proteinogenic amino acids.

Nanopore sequencing of DNA is performed by threading single-stranded DNA (ssDNA) through a narrow pore and measuring electrical signatures of the four bases — tiny perturbations, unique to each base, in a current flowing through the pore1,2. Could a similar approach be used to sequence proteins? Perhaps, but the problem is much less tractable. Proteins are chemically more complex than DNA, with 20 amino acids rather than four bases. In addition, proteins are more compact and heterogeneously charged, and must be unfolded for pore threading3. In this issue, Ouldali et al.4 describe an important step toward single-molecule protein sequencing with nanopores by outlining an approach for electrically identifying the 20 proteinogenic amino acids attached to a short peptide carrier.

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Fig. 1: Electrical recognition of amino acid residues.

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Authors and Affiliations

  1. Department of Chemistry, Institute of Structural and Molecular Biology, University College London, London, UK

    Stefan Howorka

  2. Department of Physics and Astronomy, University of California, Irvine, Irvine, California, USA

    Zuzanna S. Siwy

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  1. Stefan Howorka
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  2. Zuzanna S. Siwy
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Correspondence to Stefan Howorka or Zuzanna S. Siwy.

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Competing interests

S.H. holds patents on protein and DNA nanopores that have been licensed to Oxford Nanopore Technologies.

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Howorka, S., Siwy, Z.S. Reading amino acids in a nanopore. Nat Biotechnol 38, 159–160 (2020). https://doi.org/10.1038/s41587-019-0401-y

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