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Details

Autor(en) / Beteiligte
Titel
A turn-on fluorescent probe based on ESIPT and AIEE mechanisms for the detection of butyrylcholinesterase activity in living cells and in non-alcoholic fatty liver of zebrafish
Ist Teil von
  • Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy, 2023-02, Vol.287, p.122044, Article 122044
Ort / Verlag
Elsevier B.V
Erscheinungsjahr
2023
Quelle
Alma/SFX Local Collection
Beschreibungen/Notizen
  • [Display omitted] •An ESIPT and AIEE fluorescent probe for detecting BChE was designed.•The probe has high sensitivity and low limit for BChE.•The probe was turn-on, low background and has big Stocks shift.•The probe for BChE detection applied to cell and zebrafish imaging. Butyrylcholinesterase (BChE) and acetylcholinesterase (AChE) are two important cholinesterase enzymes in human metabolism which are closely related to various diseases of the liver. BChE and AChE are difficult to be distinguished due to their similarity in biochemical properties. Therefore, developing BChE-specific probes with high sensitivity and low background reading is desirable for the relevant biological applications. Herein, we reported the design and synthesis of a fluorescent probe HBT-BChE for biological detection and imaging of BChE. The probe is triggered by BChE-mediated hydrolysis, releasing a fluorophore that holds AIEE and ESIPT properties with large Stokes shift (>100 nm), rendering the probe features of low background interference and high sensitivity. The probe can also distinguish BChE from AChE with a low detection limit of 7.540 × 10−4 U/mL. Further in vitro studies have shown the ability of HBT-BChE to detect intracellular BChE activity, as well as to evaluate the efficiency of the BChE inhibitor. More importantly, the in vivo studies of imaging the BChE activity level in liver tissues using zebrafish as the model animal demonstrated the potential of HBT-BChE as a powerful tool for non-alcoholic fatty liver disease.
Sprache
Englisch
Identifikatoren
ISSN: 1386-1425
DOI: 10.1016/j.saa.2022.122044
Titel-ID: cdi_crossref_primary_10_1016_j_saa_2022_122044

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