Detection of oligomers and fibrils of α-synuclein by AIEgen with strong fluorescence

Leung, Chi Man; Guo, Feng; Hong, Yuning; Zhao, Engui; Kwok, Ryan T. K.; Leung, Nelson; Chen, Sijie; Vaikath, Nishant N.; El-Agnaf, Omar M. A.; Tang, Youhong; Gai, Wei-Ping; Tang, Ben Zhong

doi:10.1039/c4cc07911f

Cited by 77 publications

(82 citation statements)

References 49 publications

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“…Furthermore, the conformational specificity of these antibodies have been utilized to detect α‐syn aggregates in biochemical studies (Leung et al . ), in neurons of Caenorhabditis elegans (Kim et al . ) and rats (Duffy et al .…”

Section: α‐Syn Specific Antibodies: Invaluable Tools For Synucleinopamentioning

confidence: 99%

Antibodies against alpha‐synuclein: tools and therapies

Vaikath

Hmila

Gupta

et al. 2019

Journal of Neurochemistry

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Synucleinopathies including Parkinson's disease, dementia with Lewy bodies and multiple system atrophy are characterized by the abnormal accumulation and propagation of α‐synuclein (α‐syn) pathology in the central and peripheral nervous system as Lewy bodies or glial cytoplasmic inclusions. Several antibodies against α‐syn have been developed since it was first detected as the major component of Lewy bodies and glial cytoplasmic inclusions. Over the years, researchers have generated specific antibodies that alleviate the accumulation of intracellular aggregated α‐syn and associated pathology in cellular and preclinical models of synucleinopathies. So far, antibodies have been the first choice as tools for research and diagnosis and currently, a wide variety of antibody fragments have been developed as an alternative to full‐length antibodies for increasing its therapeutic usefulness. Recently, conformation specific antibody‐based approaches have been found to be promising as therapeutic strategies, both to block α‐syn aggregation and ameliorate the resultant cytotoxicity, and as diagnostic tools. In this review, we summarize different α‐syn specific antibodies and provide their usefulness in tackling synucleinopathies. This article is part of the Special Issue “Synuclein”.

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Section: α‐Syn Specific Antibodies: Invaluable Tools For Synucleinopamentioning

confidence: 99%

Antibodies against alpha‐synuclein: tools and therapies

Vaikath

Hmila

Gupta

et al. 2019

Journal of Neurochemistry

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Section: Probing Polymer Conformational Transitions Of Proteinsmentioning

confidence: 99%

“…TPE‐TPP, a cationic AIEgen (contrary to anionic BSPOTPE), proved to be especially useful in the analysis of early‐stage protein aggregation (Figure ) . In comparison with ThT, the AIEgen showed improved fluorescence contrast during fibrillation of the α‐Syn protein (Figure B) . Fluorescence generation is highly sensitive to ordered aggregation species, and is strictly nonresponsive to molten globules states or amorphously aggregating species, for example, in the case of RCM α‐LA protein (Figure C).…”

Section: Probing Polymer Conformational Transitions Of Proteinsmentioning

confidence: 99%

“…Inset: expansion at t= 0 to 40 h. Reproduced from ref. with permission from RSC Publishing. C) In situ TPE‐TPP assay of a molten globule (black open circle), apo (blue circle), holo (red triangle), and amyloid fibril‐forming reduced and carboxymethylated (RCM) α‐lactalbumin (α‐LA; black circle).…”

Section: Probing Polymer Conformational Transitions Of Proteinsmentioning

confidence: 99%

“…[76] The use of AIEgensi nt his field was initially inspired by the ability of AIEgen to discriminate different phases of compounds in the solid state. To date, studies have been mainlyc arried out on model fibrillation processes, including those of insulin, [77] a-synuclein( a-Syn), [78] and alpha-beta amyloids. [79] Hong and co-workersu sed BSPOTPE to study the fibrillation process of insulin ex situ (Figure 15).…”

Section: Aggregation and Fibrillation Of Proteinsmentioning

confidence: 99%

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Fluorogenic Detection and Characterization of Proteins by Aggregation‐Induced Emission Methods

Xie

Wong

Chen

et al. 2019

Chemistry A European J

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Protein is one of the four most important biomacromolecules in living systems. The detection, quantification, localization, and characterization of proteins is essential for an understanding of biological fundamentals, as well as for the diagnostics and treatment of protein‐related diseases. By using intrinsic and extrinsic fluorescence, different techniques have been established to study proteins, many of which are now being routinely used in research laboratories and clinics. This review summarizes the applications of aggregation‐induced emission (AIE) fluorescence in protein science. In contrast to traditional fluorescent dyes, the activation of AIE dyes is mainly attributed to the restriction of intramolecular motions. This unique turn‐on mechanism of AIE dyes allows researchers to develop novel fluorogenic strategies for sensitive, selective, and reliable analysis of proteins. This review focuses on introducing AIE strategies for 1) detection, localization, and quantification of proteins; 2) probing polymer conformational transitions of proteins; 3) characterization of protein–ligand interactions; and 4) evaluation of enzyme activities. Perspectives and challenges with respect to this emerging field of protein characterization are offered.

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