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FraC nanopores with adjustable diameter identify the mass of opposite-charge peptides with 44 dalton resolution

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  • Gang Huang

    (University of Groningen)

  • Arnout Voet

    (University of Leuven)

  • Giovanni Maglia

    (University of Groningen)

Abstract

A high throughput single-molecule method for identifying peptides and sequencing proteins based on nanopores could reduce costs and increase speeds of sequencing, allow the fabrication of portable home-diagnostic devices, and permit the characterization of low abundance proteins and heterogeneity in post-translational modifications. Here we engineer the size of Fragaceatoxin C (FraC) biological nanopore to allow the analysis of a wide range of peptide lengths. Ionic blockades through engineered nanopores distinguish a variety of peptides, including two peptides differing only by the substitution of alanine with glutamate. We also find that at pH 3.8 the depth of the peptide current blockades scales with the mass of the peptides irrespectively of the chemical composition of the analyte. Hence, this work shows that FraC nanopores allow direct readout of the mass of single peptide in solution, which is a crucial step towards the developing of a real-time and single-molecule protein sequencing device.

Suggested Citation

  • Gang Huang & Arnout Voet & Giovanni Maglia, 2019. "FraC nanopores with adjustable diameter identify the mass of opposite-charge peptides with 44 dalton resolution," Nature Communications, Nature, vol. 10(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-08761-6
    DOI: 10.1038/s41467-019-08761-6
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    Cited by:

    1. Smrithi Krishnan R & Kalyanashis Jana & Amina H. Shaji & Karthika S. Nair & Anjali Devi Das & Devika Vikraman & Harsha Bajaj & Ulrich Kleinekathöfer & Kozhinjampara R. Mahendran, 2022. "Assembly of transmembrane pores from mirror-image peptides," Nature Communications, Nature, vol. 13(1), pages 1-13, December.
    2. Fushi Wang & Chunxiao Zhao & Pinlong Zhao & Fanfan Chen & Dan Qiao & Jiandong Feng, 2023. "MoS2 nanopore identifies single amino acids with sub-1 Dalton resolution," Nature Communications, Nature, vol. 14(1), pages 1-8, December.
    3. Gonçalo Paulo & Ke Sun & Giovanni Di Muccio & Alberto Gubbiotti & Blasco Morozzo della Rocca & Jia Geng & Giovanni Maglia & Mauro Chinappi & Alberto Giacomello, 2023. "Hydrophobically gated memristive nanopores for neuromorphic applications," Nature Communications, Nature, vol. 14(1), pages 1-9, December.

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