Detection of phosphorylation post-translational modifications along single peptides with nanopores

Ian C. Nova; Justas Ritmejeris; Henry Brinkerhoff; Theo J.R. Koenig; Jens H. Gundlach; Cees Dekker

doi:10.1038/s41587-023-01839-z

Detection of phosphorylation post-translational modifications along single peptides with nanopores

Ian C. Nova, Justas Ritmejeris, Henry Brinkerhoff, Theo J.R. Koenig, Jens H. Gundlach, Cees Dekker^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › Scientific › peer-review

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Abstract

Current methods to detect post-translational modifications of proteins, such as phosphate groups, cannot measure single molecules or differentiate between closely spaced phosphorylation sites. We detect post-translational modifications at the single-molecule level on immunopeptide sequences with cancer-associated phosphate variants by controllably drawing the peptide through the sensing region of a nanopore. We discriminate peptide sequences with one or two closely spaced phosphates with 95% accuracy for individual reads of single molecules.

Original language	English
Pages (from-to)	710-714
Number of pages	5
Journal	Nature Biotechnology
Volume	42
Issue number	5
DOIs	https://doi.org/10.1038/s41587-023-01839-z
Publication status	Published - 2023

Bibliographical note

Green Open Access added to TU Delft Institutional Repository ‘You share, we take care!’ – Taverne project https://www.openaccess.nl/en/you-share-we-take-care Otherwise as indicated in the copyright section: the publisher is the copyright holder of this work and the author uses the Dutch legislation to make this work public.

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title = "Detection of phosphorylation post-translational modifications along single peptides with nanopores",

abstract = "Current methods to detect post-translational modifications of proteins, such as phosphate groups, cannot measure single molecules or differentiate between closely spaced phosphorylation sites. We detect post-translational modifications at the single-molecule level on immunopeptide sequences with cancer-associated phosphate variants by controllably drawing the peptide through the sensing region of a nanopore. We discriminate peptide sequences with one or two closely spaced phosphates with 95% accuracy for individual reads of single molecules.",

author = "Nova, {Ian C.} and Justas Ritmejeris and Henry Brinkerhoff and Koenig, {Theo J.R.} and Gundlach, {Jens H.} and Cees Dekker",

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doi = "10.1038/s41587-023-01839-z",

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AU - Ritmejeris, Justas

AU - Brinkerhoff, Henry

AU - Koenig, Theo J.R.

AU - Gundlach, Jens H.

AU - Dekker, Cees

N1 - Green Open Access added to TU Delft Institutional Repository ‘You share, we take care!’ – Taverne project https://www.openaccess.nl/en/you-share-we-take-care Otherwise as indicated in the copyright section: the publisher is the copyright holder of this work and the author uses the Dutch legislation to make this work public.

PY - 2023

Y1 - 2023

N2 - Current methods to detect post-translational modifications of proteins, such as phosphate groups, cannot measure single molecules or differentiate between closely spaced phosphorylation sites. We detect post-translational modifications at the single-molecule level on immunopeptide sequences with cancer-associated phosphate variants by controllably drawing the peptide through the sensing region of a nanopore. We discriminate peptide sequences with one or two closely spaced phosphates with 95% accuracy for individual reads of single molecules.

AB - Current methods to detect post-translational modifications of proteins, such as phosphate groups, cannot measure single molecules or differentiate between closely spaced phosphorylation sites. We detect post-translational modifications at the single-molecule level on immunopeptide sequences with cancer-associated phosphate variants by controllably drawing the peptide through the sensing region of a nanopore. We discriminate peptide sequences with one or two closely spaced phosphates with 95% accuracy for individual reads of single molecules.

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JO - Nature Biotechnology

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ER -

Detection of phosphorylation post-translational modifications along single peptides with nanopores

Abstract

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