文献类型：期刊文献

英文题名：Rational Design of Near-Infrared Aggregation-Induced-Emission-Active Probes: In Situ Mapping of Amyloid-β Plaques with Ultrasensitivity and High-Fidelity

作者：Fu, Wei[1]; Yan, Chenxu[1]; Guo, Zhiqian[1]; Zhang, Jingjing[2]; Zhang, Haiyan[2]; Tian, He[1]; Zhu, Wei-Hong[1]

机构：[1] Key Laboratory for Advanced Materials, Joint International Research Laboratory of Precision Chemistry and Molecular Engineering, Feringa Nobel Prize Scientist Joint Research Center, Shanghai Key Laboratory of Functional Materials Chemistry, Institute of Fine Chemicals, School of Chemistry and Molecular Engineering, East China University of Science and Technology, Shanghai, 200237, China; [2] CAS, Key Laboratory of Receptor Research, State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, 201203, China

年份：2019

卷号：141

期号：7

起止页码：3171

外文期刊名：Journal of the American Chemical Society

收录：EI(收录号：20191006589730)

语种：英文

外文关键词：Probes - Signal to noise ratio - Neurodegenerative diseases - Glycoproteins - Bridges - Infrared devices - Binding energy

摘要：High-fidelity mapping of amyloid-β (Aβ) plaques is critical for the early detection of Alzheimer's disease. However, in vivo probing of Aβ plaques by commercially available thioflavin derivatives (ThT or ThS) has proven to be extremely limited, as evident by the restriction of enrichment quenching effect, low signal-to-noise (S/N) ratio, and poor blood-brain barrier (BBB) penetrability. Herein, we demonstrate a rational design strategy of near-infrared (NIR) aggregation-induced emission (AIE)-active probes for Aβ plaques, through introducing a lipophilic π-conjugated thiophene-bridge for extension to NIR wavelength range with enhancement of BBB penetrability, and tuning the substituted position of the sulfonate group for guaranteeing specific hydrophilicity to maintain the fluorescence-off state before binding to Aβ deposition. Probe QM-FN-SO3 has settled well the AIE dilemma between the lipophilic requirement for longer emission and aggregation behavior from water to protein fibrillogenesis, thus making a breakthrough in high-fidelity feedback on in vivo detection of Aβ plaques with remarkable binding affinity, and serving as an efficient alternative to the commercial probe ThT or ThS. ? 2019 American Chemical Society.