ArticleChemical science2022
An antibody scanning method for the detection of α-synuclein oligomers in the serum of Parkinson's disease patients.
Article in Chemical science, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 19 citations in OpenAlex.
- Parkinson's Disease: From Bench to Bedside-Advancements in Diagnosis and Therapeutics using Pharmacogenomic Approach.Current gene therapy · 2026Review
- Using a stable protein scaffold to display peptides that bind to alpha-synuclein fibrils.Protein science : a publication of the Protein Society · 2025Article
- Ultrasensitive Protein Aggregate Quantification Assays for Neurodegenerative Diseases on the Simoa Platform.Analytical chemistry · 2025Article
- α-Synuclein oligomers form by secondary nucleation.Nature communications · 2024Article
- Molecular properties and diagnostic potential of monoclonal antibodies targeting cytotoxic α-synuclein oligomers.NPJ Parkinson's disease · 2024Article
- Improved Imaging Surface for Quantitative Single-Molecule Microscopy.ACS applied materials & interfaces · 2024Article
- A Potent Sybody Selectively Inhibits α-Synuclein Amyloid Formation by Binding to the P1 Region.Journal of medicinal chemistry · 2024Article
- Single-domain antibody-based protein degrader for synucleinopathies.Molecular neurodegeneration · 2024Article
- Single-Domain Antibody-Based Protein Degrader for Synucleinopathies.bioRxiv : the preprint server for biology · 2024Article
- Article
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Authors and funding
13 authors at 1 institution in 1 country.
Funding
Abstract
Misfolded α-synuclein oligomers are closely implicated in the pathology of Parkinson's disease and related synucleinopathies. The elusive nature of these aberrant assemblies makes it challenging to develop quantitative methods to detect them and modify their behavior. Existing detection methods use antibodies to bind α-synuclein aggregates in biofluids, although it remains challenging to raise antibodies against α-synuclein oligomers. To address this problem, we used an antibody scanning approach in which we designed a panel of 9 single-domain epitope-specific antibodies against α-synuclein. We screened these antibodies for their ability to inhibit the aggregation process of α-synuclein, finding that they affected the generation of α-synuclein oligomers to different extents. We then used these antibodies to investigate the size distribution and morphology of soluble α-synuclein aggregates in serum and cerebrospinal fluid samples from Parkinson's disease patients. Our results indicate that the approach that we present offers a promising route for the development of antibodies to characterize soluble α-synuclein aggregates in biofluids.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.