Site-specific post-translational modification detection by polar charged engineered MspA nanopores.

Shijun Lin, Yakun Yi, Yiheng Liu, Minglun Li, Fan Xia, Hai-Chen Wu, Xiaoding Lou

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Article in Chemical science, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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7 authors.

Shijun LinState Key Laboratory of Geomicrobiology and Environmental Changes, Faculty of Materials Science and Chemistry, China University of Geosciences Wuhan 430074 China louxiaoding@cug.edu.cn xiafan@cug.edu.cn.

Yakun YiBeijing National Laboratory for Molecular Sciences, Key Laboratory of Analytical Chemistry for Living Biosystems, Institute of Chemistry, Chinese Academy of Sciences Beijing 100190 China haichenwu@iccas.ac.cn.ORCID https://orcid.org/0000-0002-6069-867X

Yiheng LiuState Key Laboratory of Geomicrobiology and Environmental Changes, Faculty of Materials Science and Chemistry, China University of Geosciences Wuhan 430074 China louxiaoding@cug.edu.cn xiafan@cug.edu.cn.

Minglun LiState Key Laboratory of Polymer Science and Technology, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences Changchun 130022 China.ORCID https://orcid.org/0000-0002-1286-6915

Fan XiaState Key Laboratory of Geomicrobiology and Environmental Changes, Faculty of Materials Science and Chemistry, China University of Geosciences Wuhan 430074 China louxiaoding@cug.edu.cn xiafan@cug.edu.cn.ORCID https://orcid.org/0000-0001-7705-4638

Hai-Chen WuBeijing National Laboratory for Molecular Sciences, Key Laboratory of Analytical Chemistry for Living Biosystems, Institute of Chemistry, Chinese Academy of Sciences Beijing 100190 China haichenwu@iccas.ac.cn.ORCID https://orcid.org/0000-0002-4934-8521

Xiaoding LouState Key Laboratory of Geomicrobiology and Environmental Changes, Faculty of Materials Science and Chemistry, China University of Geosciences Wuhan 430074 China louxiaoding@cug.edu.cn xiafan@cug.edu.cn.ORCID https://orcid.org/0000-0002-6556-2034

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Deciphering the complex chemical code of post-translational modifications (PTMs) is fundamental to proteomics but remains challenging due to the low abundance of modified proteins and the difficulty in resolving isobaric positional isomers. Conventional mass spectrometry and affinity-based methods often lack the sensitivity or specificity required to capture this full chemical diversity. Here, we present a general strategy for site-specific PTM recognition based on MspA nanopores engineered with polar charged residues. By systematically tuning the constriction site (position N91) with polar charged residues, we introduced specific electrostatic, electroosmotic flow and steric interactions that dramatically enhance molecular recognition capabilities. This engineered interface enabled the label-free discrimination of 10 distinct PTM types across 26 peptides, including phosphorylation, glycosylation, and-reported here for the first time

Identifiers

PMID42157890

DOI10.1039/d6sc01451h

PMCPMC13181436

What Socratic holds

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LicenceCC BY-NC

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.