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Identification of single amino acid differences in uniformly charged homopolymeric peptides with aerolysin nanopore

Author

Listed:
  • Fabien Piguet

    (Université de Cergy-Pontoise)

  • Hadjer Ouldali

    (Université de Cergy-Pontoise)

  • Manuela Pastoriza-Gallego

    (Université de Cergy-Pontoise)

  • Philippe Manivet

    (Hôpital Lariboisière
    Hôpital Lariboisière)

  • Juan Pelta

    (Université d’Evry-Val-d’Essonne)

  • Abdelghani Oukhaled

    (Université de Cergy-Pontoise)

Abstract

There are still unmet needs in finding new technologies for biomedical diagnostic and industrial applications. A technology allowing the analysis of size and sequence of short peptide molecules of only few molecular copies is still challenging. The fast, low-cost and label-free single-molecule nanopore technology could be an alternative for addressing these critical issues. Here, we demonstrate that the wild-type aerolysin nanopore enables the size-discrimination of several short uniformly charged homopeptides, mixed in solution, with a single amino acid resolution. Our system is very sensitive, allowing detecting and characterizing a few dozens of peptide impurities in a high purity commercial peptide sample, while conventional analysis techniques fail to do so.

Suggested Citation

  • Fabien Piguet & Hadjer Ouldali & Manuela Pastoriza-Gallego & Philippe Manivet & Juan Pelta & Abdelghani Oukhaled, 2018. "Identification of single amino acid differences in uniformly charged homopolymeric peptides with aerolysin nanopore," Nature Communications, Nature, vol. 9(1), pages 1-13, December.
  • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-03418-2
    DOI: 10.1038/s41467-018-03418-2
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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. Parisa Bayat & Charlotte Rambaud & Bernard Priem & Matthieu Bourderioux & Mélanie Bilong & Salomé Poyer & Manuela Pastoriza-Gallego & Abdelghani Oukhaled & Jérôme Mathé & Régis Daniel, 2022. "Comprehensive structural assignment of glycosaminoglycan oligo- and polysaccharides by protein nanopore," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
    3. 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.
    4. Mohammad Ahmad & Jeung-Hoi Ha & Lauren A. Mayse & Maria F. Presti & Aaron J. Wolfe & Kelsey J. Moody & Stewart N. Loh & Liviu Movileanu, 2023. "A generalizable nanopore sensor for highly specific protein detection at single-molecule precision," Nature Communications, Nature, vol. 14(1), pages 1-14, December.
    5. Pingping Fan & Zhenyuan Cao & Shanyu Zhang & Yuqin Wang & Yunqi Xiao & Wendong Jia & Panke Zhang & Shuo Huang, 2024. "Nanopore analysis of cis-diols in fruits," Nature Communications, Nature, vol. 15(1), pages 1-15, December.

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