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<p>Fluorogenic probes capable of distinguishing enzyme activity between species are crucial for precise detection in complex biological environments. Herein, we present 5-(Pentafluorobenzoylamino) Fluorescein di-β-D-galactopyranoside (PFB-FDG), a substrate selectively activated by human β-galactosidase (β-gal) without cross-reactivity with bacterial β-gal. We tested PFB-FDG under various control conditions using purified enzymes and live cells to demonstrate that it does not activate in the presence of bacterial β-gal. Moreover, molecular docking studies suggest that the selectivity results from steric hindrance within the smaller binding pocket of bacterial β-gal, in contrast to the larger binding pocket of the human enzyme. This species-selective probe represents a major advancement, with its unique properties providing a valuable tool for future studies on human-bacterial interactions.</p>

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Species-selective activation of a β-galactosidase fluorogenic probe

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2025年7月2日

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  • Kaja Jaskot,
  • Angelika Mielcarek,
  • Łukasz Popenda,
  • Ahmet Kertmen,
  • Bartosz F. Grześkowiak,
  • Jan Barciszewski,
  • Patrick M. Perrigue

摘要

Fluorogenic probes capable of distinguishing enzyme activity between species are crucial for precise detection in complex biological environments. Herein, we present 5-(Pentafluorobenzoylamino) Fluorescein di-β-D-galactopyranoside (PFB-FDG), a substrate selectively activated by human β-galactosidase (β-gal) without cross-reactivity with bacterial β-gal. We tested PFB-FDG under various control conditions using purified enzymes and live cells to demonstrate that it does not activate in the presence of bacterial β-gal. Moreover, molecular docking studies suggest that the selectivity results from steric hindrance within the smaller binding pocket of bacterial β-gal, in contrast to the larger binding pocket of the human enzyme. This species-selective probe represents a major advancement, with its unique properties providing a valuable tool for future studies on human-bacterial interactions.