Journal
ACS SENSORS
Volume 5, Issue 6, Pages 1726-1733Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acssensors.0c00393
Keywords
bioluminescence; nanosensor; enzymatic assay; hyaluronidase; signal amplification; in vivo bioimaging
Funding
- National Natural Science Foundation of China [21735001, 21974013, 21804012, 91853104]
- Scientific Research Fund of Hunan Provincial Education Department [18B158]
- Open Fund of State Key Laboratory of Chemo/Biosensing and Chemometrics of Hunan University [2018009]
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Hyaluronidase 1 (Hyal-1) is an important enzyme involved in intracellular hyaluronic acid (HA) catabolism for performing various physiological functions, and its aberrant level is closely associated with many malignant diseases. Bioluminescence imaging is advantageous for monitoring Hyal-1 activity in vivo, but it remains challenging to design an available probe for differentiating Hyal-1 from other isoforms by a traditional strategy that covalently masks the firefly luciferase substrate. Herein, we, for the first time, present a noncovalently caging approach to construct a Hyal-1-specific bioluminogenic nanosensor by entrapping D-luciferin (D-Luc) inside the cholesterylamine-modified HA (CHA) nanoassembly to inhibit the bioluminescence production. When encountered with intracellular Hyal-1, CHA could be fully dissembled to liberate multiple copies of the loaded D-Luc, thereby emitting light by the luciferase-catalyzed bioluminescence reaction. Because of its cascade signal amplification feature, D-Luc@CHA displayed a remarkable turn-on response (248-fold) to 5 mu g/mL Hyal-1 with a detection limit of 0.07 ng/mL. Importantly, bioluminescence imaging results validated that D-Luc@CHA could be competent for dynamically visualizing endogenous Hyal-1 changes in living cells and animals and possessed the capability of discriminating between normal and cancer cells, thus offering a promising toolbox to evaluate Hyal-1 roles in biological processes as well as to diagnose Hyal-1-related diseases.
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