Nanopore-Based Protein Identification
| Autor: | Mazdak Afshar Bakshloo, John J. Kasianowicz, Manuela Pastoriza-Gallego, Jérôme Mathé, Régis Daniel, Fabien Piguet, Abdelghani Oukhaled |
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| Přispěvatelé: | Laboratoire Analyse, Modélisation et Matériaux pour la Biologie et l'Environnement (LAMBE - UMR 8587), Université d'Évry-Val-d'Essonne (UEVE)-Institut de Chimie du CNRS (INC)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-CY Cergy Paris Université (CY), ANR-17-CE09-0032,PurPepSize,Nanosenseur pour la discrimination en taille et l'analyse de pureté de peptides(2017) |
| Rok vydání: | 2022 |
| Předmět: |
Pore Forming Cytotoxic Proteins
Proteomics Myoglobin Bacterial Toxins Cytochromes c General Chemistry Biochemistry Peptide Fragments Catalysis Aeromonas hydrophila Hemolysin Proteins Nanopores Colloid and Surface Chemistry Proteolysis Muramidase Trypsin [PHYS.PHYS.PHYS-CHEM-PH]Physics [physics]/Physics [physics]/Chemical Physics [physics.chem-ph] ComputingMilieux_MISCELLANEOUS |
| Zdroj: | Journal of the American Chemical Society Journal of the American Chemical Society, 2022, 144 (6), pp.2716-2725. ⟨10.1021/jacs.1c11758⟩ |
| ISSN: | 1520-5126 0002-7863 |
| DOI: | 10.1021/jacs.1c11758 |
| Popis: | The implementation of a reliable, rapid, inexpensive, and simple method for whole-proteome identification would greatly benefit cell biology research and clinical medicine. Proteins are currently identified by cleaving them with proteases, detecting the polypeptide fragments with mass spectrometry, and mapping the latter to sequences in genomic/proteomic databases. Here, we demonstrate that the polypeptide fragments can instead be detected and classified at the single-molecule limit using a nanometer-scale pore formed by the protein aerolysin. Specifically, three different water-soluble proteins treated with the same protease, trypsin, produce different polypeptide fragments defined by the degree by which the latter reduce the nanopore's ionic current. The fragments identified with the aerolysin nanopore are consistent with the predicted fragments that trypsin could produce. |
| Databáze: | OpenAIRE |
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