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

• DOI: 10.1038/s41467-018-03418-2
• Publication Date: 2018-02-28T11:42:50Z
• Authors: Fabien Piguet; Hadjer Ouldali; Manuela Pastoriza...; Philippe Manivet; Juan Pelta; Abdelghani Oukhaled
• Keywords: Pore Forming Cytotoxic Proteins; Polymers; polymer; Science; Bacterial Toxins; arginine; chemistry; 530; 01 natural sciences; Article; pore forming cytotoxic protein; Nanopores; aerolysin; bacterial toxin; Nanotechnology; molecular analysis; controlled study; nanopore; toxin; intermethod comparison; peptide analysis; analytic method; lysine; Q; 600; particle size; peptide; 0104 chemical sciences; [CHIM.THEO]Chemical Sciences/Theoretical and/or physical chemistry; technology; [PHYS.PHYS.PHYS-CHEM-PH]Physics [physics]/Physics [physics]/Chemical Physics [physics.chem-ph]; Peptides; amino acid

AbstractThere 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.