ArticleAnalytical chemistry2018
Extrinsic Amyloid-Binding Dyes for Detection of Individual Protein Aggregates in Solution.
Article in Analytical chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Thermodynamic Frontiers in Hemoglobin-Inspired Polymer Science for Diagnosis and Modulation of Neurodegenerative Diseases.Cell biochemistry and function · 2026Review
- Multi-Spectroscopic and Molecular Modeling Studies of Interactions Between Anionic Porphyrin and Human Serum Albumin.International journal of molecular sciences · 2024Article
- In Vitro Cell Model Investigation of Alpha-Synuclein Aggregate Morphology Using Spectroscopic Imaging.International journal of molecular sciences · 2024Article
- Fibrinaloid Microclots and Atrial Fibrillation.Biomedicines · 2024Review
- Navigating the Expansive Landscapes of Soft Materials: A User Guide for High-Throughput Workflows.ACS polymers Au · 2023Review
- Single-Molecule Two-Color Coincidence Detection of Unlabeled alpha-Synuclein Aggregates.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2023Article
- Single-Molecule Two-Color Coincidence Detection of Unlabeled alpha-Synuclein Aggregates.Angewandte Chemie (International ed. in English) · 2023Article
- A review of the current research on in vivo and in vitro detection for alpha-synuclein: a biomarker of Parkinson's disease.Analytical and bioanalytical chemistry · 2023Review
- Imaging protein aggregates in the serum and cerebrospinal fluid in Parkinson's disease.Brain : a journal of neurology · 2022Article
- Single-Molecule Counting Coupled to Rapid Amplification Enables Detection of α-Synuclein Aggregates in Cerebrospinal Fluid of Parkinson's Disease Patients.Angewandte Chemie (International ed. in English) · 2021Article
- A Comparative Photophysical Study of Structural Modifications of Thioflavin T-Inspired Fluorophores.The journal of physical chemistry letters · 2020Article
- Prominent microglial inclusions in transgenic mouse models of α-synucleinopathy that are distinct from neuronal lesions.Acta neuropathologica communications · 2020Article
- Single-molecule detection on a portable 3D-printed microscope.Nature communications · 2019Article
- Soluble aggregates present in cerebrospinal fluid change in size and mechanism of toxicity during Alzheimer's disease progression.Acta neuropathologica communications · 2019Article
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Authors and funding
6 authors.
Funding
Abstract
Protein aggregation is a key molecular feature underlying a wide array of neurodegenerative disorders, including Alzheimer's and Parkinson's diseases. To understand protein aggregation in molecular detail, it is crucial to be able to characterize the array of heterogeneous aggregates that are formed during the aggregation process. We present here a high-throughput method to detect single protein aggregates, in solution, from a label-free aggregation reaction, and we demonstrate the approach with the protein associated with Parkinson's disease, α-synuclein. The method combines single-molecule confocal microscopy with a range of amyloid-binding extrinsic dyes, including thioflavin T and pentameric formylthiophene acetic acid, and we show that we can observe aggregates at low picomolar concentrations. The detection of individual aggregates allows us to quantify their numbers. Furthermore, we show that this approach also allows us to gain structural insights from the emission intensity of the extrinsic dyes that are bound to aggregates. By analyzing the time evolution of the aggregate populations on a single-molecule level, we then estimate the fragmentation rate of aggregates, a key process that underlies the multiplication of pathological aggregates. We additionally demonstrate that the method permits the detection of these aggregates in biological samples. The capability to detect individual protein aggregates in solution opens up a range of new applications, including exploiting the potential of this method for high-throughput screening of human biofluids for disease diagnosis and early detection.
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Registered trials
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