ArticleACS chemical neuroscience2023
Elucidation of Secondary Structure and Toxicity of α-Synuclein Oligomers and Fibrils Grown in the Presence of Phosphatidylcholine and Phosphatidylserine.
Article in ACS chemical neuroscience, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Lipid Acyl Chain-Driven α-Synuclein Fibril Polymorphisms and Neuronal Pathologies.ACS chemical neuroscience · 2026Article
- Familial mutations modulate α-synuclein interactions with key neuronal membrane lipids.The FEBS journal · 2026Article
- Elucidation of Molecular Mechanisms of Lipid-Altered Cytotoxicity of TDP-43 Fibrils.ACS chemical neuroscience · 2026Article
- Molecular mechanisms of exercise-induced neuroprotection against Parkinson's disease.Sports medicine and health science · 2026Review
- Elevated hexosylceramides in Parkinson's disease cause gene upregulations in neurons mimicking responses to pathogens.NPJ Parkinson's disease · 2025Article
- Comparative Analysis of Aggregation of β- and γ-Synucleins in Vertebrates.Biomolecules · 2025Article
- The role of phospholipid saturation and composition in α-synuclein aggregation and toxicity: A dual in vitro and in vivo approach.Protein science : a publication of the Protein Society · 2025Article
- Elucidation of cytotoxicity of α-Synuclein fibrils on immune cells.Biochimica et biophysica acta. Proteins and proteomics · 2025Article
- Tubulin-Binding Region Modulates Cholesterol-Triggered Aggregation of Tau Proteins.Journal of neurochemistry · 2025Article
- Integrated metabolomic-lipidomic profiling reveals novel biomarkers and therapeutic targets for alcohol use disorder with cognitive impairment.Frontiers in psychiatry · 2025Article
- Cholesterol Accelerates Aggregation of α-Synuclein Simultaneously Increasing the Toxicity of Amyloid Fibrils.ACS chemical neuroscience · 2024Article
- Elucidating the mechanisms of α-Synuclein-lipid interactions using site-directed mutagenesis.Neurobiology of disease · 2024Article
- Tubulin-binding region alters tau-lipid interactions and changes toxicity of tau fibrils formed in the presence of phosphatidylserine lipids.Protein science : a publication of the Protein Society · 2024Article
- Length and saturation of choline plasmalogens alter the aggregation rate of α-synuclein but not the toxicity of amyloid fibrils.International journal of biological macromolecules · 2024Article
- Large Unilamellar Vesicles of Phosphatidic Acid Reduce the Toxicity of α-Synuclein Fibrils.Molecular pharmaceutics · 2024Article
- The influence of zwitterionic and anionic phospholipids on protein aggregation.Biophysical chemistry · 2024Review
- Exploring the causal effects of serum lipids and lipidomes on lewy body dementia: a Mendelian randomization study.Frontiers in endocrinology · 2024Article
- Novel strategies in Parkinson's disease treatment: a review.Frontiers in molecular neuroscience · 2024Review
- The causal role of lipids in dementia: A Mendelian randomization study.Journal of Alzheimer's disease reportsArticle
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3 authors.
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Abstract
Abrupt aggregation of α-synuclein (α-Syn) in the midbrain hypothalamus and thalamus is a hallmark of Parkinson's disease (PD), the fastest growing neurodegenerative pathology, projected to strike 12 million people by 2040 worldwide. In this study, we examine the effect of two phospholipids that are present in neuronal membranes, phosphatidylcholine (PC) and phosphatidylserine (PS), on the rate of α-Syn aggregation. We found that PS accelerated α-Syn aggregation, whereas PC strongly inhibited α-Syn aggregation. We also utilized the nano-infrared imaging technique, also known as atomic force microscopy infrared (AFM-IR) spectroscopy, to investigate whether PC and PS only change the rates or also modify the secondary structure of α-Syn aggregates. We found that both phospholipids uniquely altered the secondary structure of α-Syn aggregates present at the lag and growth phase, as well as the late stage of protein aggregation. In addition, compared to the α-Syn aggregates formed in the lipid-free environment, α-Syn:PC and α-Syn:PS aggregates demonstrated higher cellular toxicity to N27 rat neurons. Interestingly, both α-Syn:PC and α-Syn:PS aggregates showed similar levels of oxidative stress, but α-Syn:PC aggregates exhibited a greater degree of mitochondrial dysfunction compared to α-Syn:PS aggregates.
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