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<p>A novel signal-switchable fluorescent biosensing platform was rationally developed based on oxidized single-walled carbon nanohorns (oxSWCNHs) and FAM-labeled peptide probes for the highly sensitive detection, activity evaluation, and intracellular bioimaging of histone deacetylase 1 (HDAC1). The FAM-modified peptide substrate could be tightly adsorbed on the oxSWCNHs. In the presence of HDAC1, the specific deacetylation of acetyl-lysine residues initiated the sequential enzymatic cleavage reaction triggered by carboxypeptidase Y (CPY), which led to the detachment of fluorophores from oxSWCNHs and the obvious recovery of fluorescence signals. Under optimized experimental conditions, the constructed biosensor exhibited excellent sensing performance toward HDAC1 with a low detection limit of 1.4&#xa0;ng/mL. Meanwhile, the sensing system was effectively utilized to precisely detect HDAC1 in the serum of humans, quantitatively assess the inhibitory effect of trichostatin A (TSA), and achieve intracellular fluorescence imaging of endogenous HDAC1 in living cells. Featuring high sensitivity, favorable specificity, and simple operation, this fluorescent sensing strategy provides a promising and universal tool for clinical HDAC1 analysis, disease-related research and inhibitor screening.</p> Graphical abstract <p></p>

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Activatable fluorescent nanosensor for real-time detection and intracellular imaging of histone deacetylase 1

  • 期刊论文

  • 发表日期：

    2026年6月29日

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  • Zhifeng Wang,
  • Jiangnan Wang,
  • Yu Huang,
  • Dezhi Zhao,
  • Tingting Feng

摘要

A novel signal-switchable fluorescent biosensing platform was rationally developed based on oxidized single-walled carbon nanohorns (oxSWCNHs) and FAM-labeled peptide probes for the highly sensitive detection, activity evaluation, and intracellular bioimaging of histone deacetylase 1 (HDAC1). The FAM-modified peptide substrate could be tightly adsorbed on the oxSWCNHs. In the presence of HDAC1, the specific deacetylation of acetyl-lysine residues initiated the sequential enzymatic cleavage reaction triggered by carboxypeptidase Y (CPY), which led to the detachment of fluorophores from oxSWCNHs and the obvious recovery of fluorescence signals. Under optimized experimental conditions, the constructed biosensor exhibited excellent sensing performance toward HDAC1 with a low detection limit of 1.4 ng/mL. Meanwhile, the sensing system was effectively utilized to precisely detect HDAC1 in the serum of humans, quantitatively assess the inhibitory effect of trichostatin A (TSA), and achieve intracellular fluorescence imaging of endogenous HDAC1 in living cells. Featuring high sensitivity, favorable specificity, and simple operation, this fluorescent sensing strategy provides a promising and universal tool for clinical HDAC1 analysis, disease-related research and inhibitor screening.

Graphical abstract