Publication

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

Huang, G., Voet, A. & Maglia, G., 19-Feb-2019, In : Nature Communications. 10, 10 p., 835.

Research output: Contribution to journalArticleAcademicpeer-review

APA

Huang, G., Voet, A., & Maglia, G. (2019). FraC nanopores with adjustable diameter identify the mass of opposite-charge peptides with 44 dalton resolution. Nature Communications, 10, [835]. https://doi.org/10.1038/s41467-019-08761-6

Author

Huang, Gang ; Voet, Arnout ; Maglia, Giovanni. / FraC nanopores with adjustable diameter identify the mass of opposite-charge peptides with 44 dalton resolution. In: Nature Communications. 2019 ; Vol. 10.

Harvard

Huang, G, Voet, A & Maglia, G 2019, 'FraC nanopores with adjustable diameter identify the mass of opposite-charge peptides with 44 dalton resolution' Nature Communications, vol. 10, 835. https://doi.org/10.1038/s41467-019-08761-6

Standard

FraC nanopores with adjustable diameter identify the mass of opposite-charge peptides with 44 dalton resolution. / Huang, Gang; Voet, Arnout; Maglia, Giovanni.

In: Nature Communications, Vol. 10, 835, 19.02.2019.

Research output: Contribution to journalArticleAcademicpeer-review

Vancouver

Huang G, Voet A, Maglia G. FraC nanopores with adjustable diameter identify the mass of opposite-charge peptides with 44 dalton resolution. Nature Communications. 2019 Feb 19;10. 835. https://doi.org/10.1038/s41467-019-08761-6


BibTeX

@article{ea77c317dd9144ff9c5fa1e1f69b903d,
title = "FraC nanopores with adjustable diameter identify the mass of opposite-charge peptides with 44 dalton resolution",
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.",
keywords = "SINGLE DNA-MOLECULES, PROTEIN, SIZE, DISCRIMINATION, RECOGNITION, IDENTIFICATION, TRANSLOCATION, SPECTROMETRY, AEROLYSIN, POLYMERS",
author = "Gang Huang and Arnout Voet and Giovanni Maglia",
year = "2019",
month = "2",
day = "19",
doi = "10.1038/s41467-019-08761-6",
language = "English",
volume = "10",
journal = "Nature Communications",
issn = "2041-1723",
publisher = "Nature Publishing Group",

}

RIS

TY - JOUR

T1 - FraC nanopores with adjustable diameter identify the mass of opposite-charge peptides with 44 dalton resolution

AU - Huang, Gang

AU - Voet, Arnout

AU - Maglia, Giovanni

PY - 2019/2/19

Y1 - 2019/2/19

N2 - 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.

AB - 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.

KW - SINGLE DNA-MOLECULES

KW - PROTEIN

KW - SIZE

KW - DISCRIMINATION

KW - RECOGNITION

KW - IDENTIFICATION

KW - TRANSLOCATION

KW - SPECTROMETRY

KW - AEROLYSIN

KW - POLYMERS

U2 - 10.1038/s41467-019-08761-6

DO - 10.1038/s41467-019-08761-6

M3 - Article

VL - 10

JO - Nature Communications

JF - Nature Communications

SN - 2041-1723

M1 - 835

ER -

ID: 77007071