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

Fabien Piguet (), Hadjer Ouldali, Manuela Pastoriza-Gallego, Philippe Manivet, Juan Pelta () and Abdelghani Oukhaled ()
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Fabien Piguet: Université de Cergy-Pontoise
Hadjer Ouldali: Université de Cergy-Pontoise
Manuela Pastoriza-Gallego: Université de Cergy-Pontoise
Philippe Manivet: Hôpital Lariboisière
Juan Pelta: Université d’Evry-Val-d’Essonne
Abdelghani Oukhaled: Université de Cergy-Pontoise

Nature Communications, 2018, vol. 9, issue 1, 1-13

Abstract: 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.

Date: 2018
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DOI: 10.1038/s41467-018-03418-2

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