41589-44-0Relevant academic research and scientific papers
Rational Design of Crystallization-Induced-Emission Probes To Detect Amorphous Protein Aggregation in Live Cells
Bai, Yulong,Dong, Xuepeng,Gao, Zhenming,Huang, Yanan,Jin, Wenhan,Liu, Xiaojing,Liu, Yu,Lyu, Haochen,Piao, Hai-Long,Shen, Di,Tang, Yuqi,Wan, Wang,Wang, Mengdie,Zeng, Lianggang
, p. 16067 - 16076 (2021)
Unlike amyloid aggregates, amorphous protein aggregates with no defined structures have been challenging to target and detect in a complex cellular milieu. In this study, we rationally designed sensors of amorphous protein aggregation from aggregation-induced-emission probes (AIEgens). Utilizing dicyanoisophorone as a model AIEgen scaffold, we first sensitized the fluorescence of AIEgens to a nonpolar and viscous environment mimicking the interior of amorphous aggregated proteins. We identified a generally applicable moiety (dimethylaminophenylene) for selective binding and fluorescence enhancement. Regulation of the electron-withdrawing groups tuned the emission wavelength while retaining selective detection. Finally, we utilized the optimized probe to systematically image aggregated proteome upon proteostasis network regulation. Overall, we present a rational approach to develop amorphous protein aggregation sensors from AIEgens with controllable sensitivity, spectral coverage, and cellular performance.
