ArticleBiophysical journal2014
Alpha-synuclein lipid-dependent membrane binding and translocation through the α-hemolysin channel.
Article in Biophysical journal, 2014. 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, 33 citations in OpenAlex.
- Antimicrobial peptide class that forms discrete β-barrel stable pores anchored by transmembrane helices.Nature communications · 2025Article
- Conformational plasticity of mitochondrial VDAC2 controls the kinetics of its interaction with cytosolic proteins.Science advances · 2025Article
- Polymorphic Alpha-Synuclein Oligomers: Characterization and Differential Detection with Novel Corresponding Antibodies.Molecular neurobiology · 2023Article
- Restricting α-synuclein transport into mitochondria by inhibition of α-synuclein-VDAC complexation as a potential therapeutic target for Parkinson's disease treatment.Cellular and molecular life sciences : CMLS · 2022Article
- Surface-facilitated trapping by active sites: From catalysts to viruses.The Journal of chemical physics · 2021Article
- 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
- Capturing single molecules by nanopores: measured times and thermodynamics.Physical chemistry chemical physics : PCCP · 2021Article
- Detailed balance for diffusion in a potential with trapping and forward-backward symmetry of trapping time distributions.The Journal of chemical physics · 2020Article
- Effect of a post-translational modification mimic on protein translocation through a nanopore.Nanoscale · 2020Article
- Exploring the Nature of Cationic Blocker Recognition by the Anthrax Toxin Channel.Biophysical journal · 2019Article
- First passage, looping, and direct transition in expanding and narrowing tubes: Effects of the entropy potential.The Journal of chemical physics · 2017Article
- A new insight into diffusional escape from a biased cylindrical trap.The Journal of chemical physics · 2017Article
- Bulk-mediated surface transport in the presence of bias.The Journal of chemical physics · 2017Article
- Mechanism of α-synuclein translocation through a VDAC nanopore revealed by energy landscape modeling of escape time distributions.Nanoscale · 2017Article
- Impact of Dendrimer Terminal Group Chemistry on Blockage of the Anthrax Toxin Channel: A Single Molecule Study.Toxins · 2016Article
- Quarterly intrinsic disorder digest (January-February-March, 2014).Intrinsically disordered proteins · 2016Article
- Tubulin tail sequences and post-translational modifications regulate closure of mitochondrial voltage-dependent anion channel (VDAC).The Journal of biological chemistry · 2015Article
- A new approach to the problem of bulk-mediated surface diffusion.The Journal of chemical physics · 2015Article
- α-Synuclein Shows High Affinity Interaction with Voltage-dependent Anion Channel, Suggesting Mechanisms of Mitochondrial Regulation and Toxicity in Parkinson Disease.The Journal of biological chemistry · 2015Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Gauging the interactions of a natively unfolded Parkinson disease-related protein, alpha-synuclein (α-syn) with membranes and its pathways between and within cells is important for understanding its pathogenesis. Here, to address these questions, we use a robust β-barrel channel, α-hemolysin, reconstituted into planar lipid bilayers. Transient, ~95% blockage of the channel current by α-syn was observed when 1), α-syn was added from the membrane side where the shorter (stem) part of the channel is exposed; and 2), the applied potential was lower on the side of α-syn addition. While the on-rate of α-syn binding to the channel strongly increased with the applied field, the off-rate displayed a turnover behavior. Statistical analysis suggests that at voltages >50 mV, a significant fraction of the α-syn molecules bound to the channel undergoes subsequent translocation. The observed on-rate varied by >100 times depending on the bilayer lipid composition. Removal of the last 25 amino acids from the highly negatively charged C-terminal of α-syn resulted in a significant decrease in the binding rates. Taken together, these results demonstrate that β-barrel channels may serve as sensitive probes of α-syn interactions with membranes as well as model systems for studies of channel-assisted protein transport.
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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.