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<p>Effective and precise detection of peptides and their post-translational modifications (PTMs) is crucial for biomedical research but remains technically challenging. Here, we present a nanopore sensing strategy that enables label-free analysis of negatively charged peptides. By introducing arginine residues into the nanopore and using amino-cyclodextrin as a molecular adaptor, the system enables unambiguous discrimination of short negatively charged homopeptides differing by only a single residue. Building on this capability, the platform further demonstrates high sensitivity for detecting representative PTMs, including acetylation, lactylation, and phosphorylation, introduced on a negatively charged peptide scaffold. Notably, the system could also analyze fragments generated by proteolytic digestion of full-length proteins, underscoring its potential for accurate protein identification. This work offers an accessible and reliable strategy to characterize peptide variants with single-amino acid differences and PTMs, which may facilitate future applications in peptide biomarker detection and protein sequence analysis.</p> Graphical abstract <p></p>

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Discriminating single-amino acid differences and post-translational modifications in negatively charged peptides with α-hemolysin nanopores

  • 期刊论文

  • 出版模式：

    开放获取

  • 发表日期：

    2026年7月21日

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  • Liting Kang,
  • Linting Wang,
  • Xuefei Fan,
  • Lingfang Xu,
  • Han Yang,
  • Chenxin Wu,
  • Tongxin Zhu,
  • Xiangyi Zhao,
  • Linming Zhang,
  • Jianhuang Xue,
  • Shuanghong Yan

摘要

Effective and precise detection of peptides and their post-translational modifications (PTMs) is crucial for biomedical research but remains technically challenging. Here, we present a nanopore sensing strategy that enables label-free analysis of negatively charged peptides. By introducing arginine residues into the nanopore and using amino-cyclodextrin as a molecular adaptor, the system enables unambiguous discrimination of short negatively charged homopeptides differing by only a single residue. Building on this capability, the platform further demonstrates high sensitivity for detecting representative PTMs, including acetylation, lactylation, and phosphorylation, introduced on a negatively charged peptide scaffold. Notably, the system could also analyze fragments generated by proteolytic digestion of full-length proteins, underscoring its potential for accurate protein identification. This work offers an accessible and reliable strategy to characterize peptide variants with single-amino acid differences and PTMs, which may facilitate future applications in peptide biomarker detection and protein sequence analysis.

Graphical abstract