ArticleBiochimica et biophysica acta. Biomembranes2018
Stimulation of α-synuclein amyloid formation by phosphatidylglycerol micellar tubules.
Article in Biochimica et biophysica acta. Biomembranes, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 26 citations in OpenAlex.
- Elucidating the mechanisms of α-Synuclein-lipid interactions using site-directed mutagenesis.Neurobiology of disease · 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
- The influence of zwitterionic and anionic phospholipids on protein aggregation.Biophysical chemistry · 2024Review
- The Effects of Lipids on α-Synuclein Aggregation In Vitro.Biomolecules · 2023Review
- Special issue for Klaus Gawrisch.Biophysical journal · 2023Article
- Molecularly imprinted sensor based on poly-o-phenylenediamine-hydroquinone polymer for β-amyloid-42 detection.Analytical and bioanalytical chemistry · 2023Article
- Effects of a Semisynthetic Catechin on Phosphatidylglycerol Membranes: A Mixed Experimental and Simulation Study.Molecules (Basel, Switzerland) · 2023Article
- An Adaptive Role for DNA Double-Strand Breaks in Hippocampus-Dependent Learning and Memory.International journal of molecular sciences · 2022Review
- First insights into the honey bee (Journal of advanced research · 2022Article
- Fat and Protein Combat Triggers Immunological Weapons of Innate and Adaptive Immune Systems to Launch Neuroinflammation in Parkinson's Disease.International journal of molecular sciences · 2022Review
- Dual Effects of Presynaptic Membrane Mimetics onFrontiers in cell and developmental biology · 2022Article
- Exploring lipid-dependent conformations of membrane-bound α-synuclein with the VDAC nanopore.Biochimica et biophysica acta. Biomembranes · 2021Article
- Regulation of Mitochondrial Respiration by VDAC Is Enhanced by Membrane-Bound Inhibitors with Disordered Polyanionic C-Terminal Domains.International journal of molecular sciences · 2021Review
- Membrane composition and lipid to protein ratio modulate amyloid kinetics of yeast prion protein.RSC chemical biology · 2021Article
- Membrane Interactions of α-Synuclein Probed by Neutrons and Photons.Accounts of chemical research · 2021Article
- Modulation of the Interactions Between α-Synuclein and Lipid Membranes by Post-translational Modifications.Frontiers in neurology · 2021Review
- Interplay between α-synuclein amyloid formation and membrane structure.Biochimica et biophysica acta. Proteins and proteomics · 2019Review
- The Role of Lipids in Parkinson's Disease.Cells · 2019Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
α-Synuclein (α-Syn) is a presynaptic protein that is accumulated in its amyloid form in the brains of Parkinson's patients. Although its biological function remains unclear, α-syn has been suggested to bind to synaptic vesicles and facilitate neurotransmitter release. Recently, studies have found that α-syn induces membrane tubulation, highlighting a potential mechanism for α-syn to stabilize highly curved membrane structures which could have both functional and dysfunctional consequences. To understand how membrane remodeling by α-syn affects amyloid formation, we have studied the α-syn aggregation process in the presence of phosphatidylglycerol (PG) micellar tubules, which were the first reported example of membrane tubulation by α-syn. Aggregation kinetics, β-sheet content, and macroscopic protein-lipid structures were observed by Thioflavin T fluorescence, circular dichroism spectroscopy and transmission electron microscopy, respectively. Collectively, the presence of PG micellar tubules formed at a stochiometric (L/P = 1) ratio was found to stimulate α-syn fibril formation. Moreover, transmission electron microscopy and solid-state nuclear magnetic resonance spectroscopy revealed the co-assembly of PG and α-syn into fibril structures. However, isolated micellar tubules do not form fibrils by themselves, suggesting an important role of free α-syn monomers during amyloid formation. In contrast, fibrils did not form in the presence of excess PG lipids (≥L/P = 50), where most of the α-syn molecules are in a membrane-bound α-helical form. Our results provide new mechanistic insights into how membrane tubules modulate α-syn amyloid formation and support a pivotal role of protein-lipid interaction in the dysfunction of α-syn.
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