Trimodal probe for proteome profiling of AchE in animals

ABSTRACT: Acetylcholinesterase (AChE) is a cholinergic enzyme that hydrolyzes esters of the neurotransmitter acetylcholine (Ach). Aberrant activity of AChE is closely associated with various neurodegenerative diseases and cancer. Current chemical probes for AChE detection mostly rely on fluorescence readout as a single-modality approach. The development of activity-based multimodal probes, which integrate the complementary advantages of near-infrared fluorescence (NIRF) imaging, photoacoustic (PA) detection, and proteome profiling, are therefore highly valuable. Such probes can provide more comprehensive information for deciphering the AChE code. Herein, we developed a set of multimodal probes, termed AFP1, AFP2, AFP3, and AFPP. AFP1/2/3, which enable NIRF/PA imaging, are capable of monitoring AChE activity in a continuous manner. AFPP is the first trimodal probe capable of NIRF/PA imaging and proteome profiling of AchE in live cells and animals. Notably, the usage of AFP2 and AFPP (1) highlights the superior capability of PA imaging for live animal studies; and (2) reveals significantly elevated AChE activity in microglia compared to astrocytes, as demonstrated in both cellular and murine models of depression.

ORGANISM(S): Mus Musculus

SUBMITTER: Yusheng Xie  

PROVIDER: PXD063264 | iProX | Thu Apr 24 00:00:00 BST 2025

REPOSITORIES: iProX