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Technique for Intranasal Administration of α-Synuclein Aggregates
Published on: November 8, 2024
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Dioleoyl-phosphatidic acid selectively binds to α-synuclein and strongly induces its aggregation
Satoru Mizuno1, Hirotaka Sasai1, Aiko Kume1
1Department of Chemistry, Graduate School of Science, Chiba University, Japan.
FEBS Letters
|February 11, 2017
Summary
The fatty acyl chains of phosphatidic acid (PA) influence alpha-synuclein (α-syn) binding. Specifically, 18:1/18:1-PA shows the strongest binding and most effectively promotes α-syn aggregation, a key process in Parkinson's disease.
Area of Science:
- Neuroscience
- Biochemistry
- Molecular Biology
Background:
- Alpha-synuclein (α-syn) aggregation is a hallmark of Parkinson's disease (PD).
- Alpha-synuclein (α-syn) interacts with phosphatidic acid (PA) on vesicles.
- The role of PA's fatty acyl chains in α-syn binding is not well understood.

