详细信息
Fluorogenic sensing of amorphous aggregates, amyloid fibers, and chaperone activity via a near-infrared aggregation-induced emission-active probe ( EI收录)
文献类型:期刊文献
英文题名:Fluorogenic sensing of amorphous aggregates, amyloid fibers, and chaperone activity via a near-infrared aggregation-induced emission-active probe
作者:He, Wei[1,5];Yang, Yuanyuan[1];Qian, Yuhui[1];Chen, Zhuoyi[1];Zheng, Yongxin[1];Zhao, Wenping[1];Yan, Chenxu[2,3];Guo, Zhiqian[2,3];Quan, Shu[1,4,6]
机构:[1]East China Univ Sci & Technol, Shanghai Collaborat Innovat Ctr Biomfg SCICB, State Key Lab Bioreactor Engn, Shanghai, Peoples R China;[2]East China Univ Sci & Technol, Inst Fine Chem, Frontiers Sci Ctr Materiobiol & Dynam Chem, Sch Chem & Mol Engn,Key Lab Adv Mat, Shanghai, Peoples R China;[3]East China Univ Sci & Technol, Inst Fine Chem, Sch Chem & Mol Engn, Frontiers Sci Ctr Materiobiol & Dynam Chem,Joint I, Shanghai, Peoples R China;[4]East China Univ Sci & Technol, Shanghai Frontiers Sci Ctr Optogenet Tech Cell Met, Shanghai, Peoples R China;[5]East China Univ Sci & Technol, Shanghai Collaborat Innovat Ctr Biomfg SCICB, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China;[6]East China Univ Sci & Technol, Shanghai Frontiers Sci Ctr Optogenet Tech Cell Met, Shanghai 200237, Peoples R China
年份:2024
卷号:5
期号:1
外文期刊名:AGGREGATE
收录:EI(收录号:20233514655742);WOS:【ESCI(收录号:WOS:001152082500001)】;
基金:This work was supported by the Natural Science Foundation of Shanghai, Grant Number: 23ZR1415300; The National Natural Science Foundation of China (NSFC), Grant Numbers: 32222049, 31661143021, 32171269, and 32201043; The National Key Research and Development Program of China, Grant Number: 2022YFF1102900; The Shanghai Frontier Science Center of Optogenetic Techniques for Cell Metabolism Shanghai Municipal Education Commission, Grant Number: 2021 Sci & Tech 03 28
语种:英文
外文关键词:aggregation-induced emission; fluorescence; molecular chaperone; protein aggregation
摘要:The presence of protein aggregates in numerous human diseases underscores the significance of detecting these aggregates to comprehend disease mechanisms and develop novel therapeutic approaches for combating these disorders. Despite the development of various biosensors and fluorescent probes that selectively target amyloid fibers or amorphous aggregates, there is still a lack of tools capable of simultaneously detecting both types of aggregates. Herein, we demonstrate the quantitative discernment of amorphous aggregates by QM-FN-SO3, an aggregation-induced emission (AIE) probe initially designed for detecting amyloid fibers. This probe easily penetrates the membranes of the widely-used prokaryotic model organism Escherichia coli, enabling the visualization of both amorphous aggregates and amyloid fibers through near-infrared fluorescence. Notably, the probe exhibits sensitivity in distinguishing the varying aggregation propensities of proteins, regardless of whether they form amorphous aggregates or amyloid fibers in vivo. These properties contribute to the successful application of the QM-FN-SO3 probe in the subsequent investigation of the antiaggregation activities of two outer membrane protein (OMP) chaperones, both in vitro and in their physiological environment. Overall, our work introduces a near-infrared fluorescent chemical probe that can quantitatively detect amyloid fibers and amorphous aggregates with high sensitivity in vitro and in vivo. Furthermore, it demonstrates the applicability of the probe in chaperone biology and its potential as a high-throughput screening tool for protein aggregation inhibitors and folding factors. This study illustrates the capacity of the AIE-based fluorescent probe QM-FN-SO3 in quantitatively detecting both amorphous and amyloid-type protein aggregates both in vitro and in vivo. The probe displays remarkable sensitivity, exceptional photostability, and excellent membrane penetrability, rendering it suitable for super-resolution imaging of protein aggregates, differentiating various protein aggregation propensities, and investigating the antiaggregation activities of protein chaperones. image
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