ArticleACS chemical neuroscience2015
Molecular determinants of α-synuclein mutants' oligomerization and membrane interactions.
Article in ACS chemical neuroscience, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- Lipid membrane remodeling by myristic acid treatment reverses Parkinson's disease α-synuclein phenotypes in patient neurons.npj metabolic health and disease · 2026Article
- Cholesterol modulates vesicle clustering mediated by alpha-synuclein in a nonlinear fashion.Biophysics reports · 2025Article
- Parkinson disease is a fatty acidopathy.Nature reviews. Neurology · 2025Review
- Self-limiting multimerization of α-synuclein on membrane and its implication in Parkinson's diseases.Science advances · 2024Article
- Curcumin Inhibits α-Synuclein Aggregation by Acting on Liquid-Liquid Phase Transition.Foods (Basel, Switzerland) · 2024Article
- Enhanced Inhibition of Amyloid Formation by Heat Shock Protein 90 Immobilized on Nanoparticles.ACS chemical neuroscience · 2023Article
- Article
- Lipase regulation of cellular fatty acid homeostasis as a Parkinson's disease therapeutic strategy.NPJ Parkinson's disease · 2022Article
- Impact of Fatty Acid-Binding Proteins in α-Synuclein-Induced Mitochondrial Injury in Synucleinopathy.Biomedicines · 2021Review
- Neurons and Glia Interplay in α-Synucleinopathies.International journal of molecular sciences · 2021Review
- Effects of pH on an IDP conformational ensemble explored by molecular dynamics simulation.Biophysical chemistry · 2021Article
- Biophysical processes underlying cross-seeding in amyloid aggregation and implications in amyloid pathology.Biophysical chemistry · 2021Review
- α-Synuclein: An All-Inclusive Trip Around its Structure, Influencing Factors and Applied Techniques.Frontiers in chemistry · 2021Review
- α-Synuclein-112 Impairs Synaptic Vesicle Recycling Consistent With Its Enhanced Membrane Binding Properties.Frontiers in cell and developmental biology · 2020Article
- Binding of α-synuclein oligomers to Cx32 facilitates protein uptake and transfer in neurons and oligodendrocytes.Acta neuropathologica · 2019Article
- Living in Promiscuity: The Multiple Partners of Alpha-Synuclein at the Synapse in Physiology and Pathology.International journal of molecular sciences · 2019Review
- Membrane binding, internalization, and sorting of alpha-synuclein in the cell.Acta neuropathologica communications · 2018Article
- Insights into the Molecular Mechanisms of Alzheimer's and Parkinson's Diseases with Molecular Simulations: Understanding the Roles of Artificial and Pathological Missense Mutations in Intrinsically Disordered Proteins Related to Pathology.International journal of molecular sciences · 2018Review
- FLZ Attenuates α-Synuclein-Induced Neurotoxicity by Activating Heat Shock Protein 70.Molecular neurobiology · 2017Article
- A de novo compound targeting α-synuclein improves deficits in models of Parkinson's disease.Brain : a journal of neurology · 2016Article
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11 authors.
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Abstract
Parkinson's disease (PD) is associated with the formation of toxic α-synuclein oligomers that can penetrate the cell membrane. Familial forms of PD are caused by the point mutations A53T, A30P, E46K, and H50Q. Artificial point mutations E35K and E57K also increase oligomerization and pore formation. We generated structural conformations of α-synuclein and the above-mentioned mutants using molecular dynamics. We elucidated four main regions in these conformers contacting the membrane and found that the region including residues 39-45 (Zone2) may have maximum membrane penetration. E57K mutant had the highest rate of interaction with the membrane, followed by A53T, E46K, and E35K mutants and wild type (wt) α-synuclein. The mutant A30P had the smallest percentage of conformers that contact the membrane by Zone 2 than all other mutants and wt α-synuclein. These results were confirmed experimentally in vitro. We identified the key amino acids that can interact with the membrane (Y38, E62, and N65 (first hydrophilic layer); E104, E105, and D115 (second hydrophilic layer), and V15 and V26 (central hydrophobic layer)) and the residues that are involved in the interprotein contacts (L38, V48, V49, Q62, and T64). Understanding the molecular interactions of α-synuclein mutants is important for the design of compounds blocking the formation of toxic oligomers.
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