A Double-Locked ESIPT-AIE Fluorescent Probe Detects Esterase with Highly Matched Response Kinetics

Analytical Chemistry, Год журнала: 2025, Номер unknown

Опубликована: Фев. 25, 2025

Hydrolyases play an irreplaceable role in complex biological processes, and their dysfunction is a cause of many human diseases. Advanced activatable situ fluorescence detection methods offer high-resolution spatiotemporal analysis, aiding the dissection roles hydrolases. However, current strategies typically focus on only specific stages enzyme-probe interactions, leading to suboptimal imaging fidelity sometimes erroneous results. Addressing this, we developed double-locked "Excited State Intramolecular Proton Transfer-Aggregation Induced Emission (ESIPT-AIE)" fluorescent probe (Br-3N-2Et) that matches entire enzymatic response kinetics for enzyme activity detection. We validated probe's mechanism by enhancing pre-reaction recognition through double unlockable sites, thereby reducing basal (Φ = 0.0183) increasing resistance interference signals. Subsequently, ESIPT fluorophore with multiple hydrogen bonds enhanced affinity hydrolase catalytic site, improving binding exhibiting significant Stokes shift (188 nm). The realization ESIPT-AIE dual-emission facilitated rapid efflux from site subsequent signal enhancement (132.2-fold). This new achieved regional differential esterase HepG2 cells endometrial cancer tissues. Thus, this work paves way development integrated, multimechanism platforms sensing biochemical contexts.

Язык: Английский

A near-infrared fluorescence probe for sensing mitochondrial viscosity in cells and mice

Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy, Год журнала: 2025, Номер unknown, С. 126175 - 126175

Опубликована: Апрель 1, 2025

Язык: Английский