ArticleThe journal of physical chemistry. B2012
Characterization of a disordered protein during micellation: interactions of α-synuclein with sodium dodecyl sulfate.
Article in The journal of physical chemistry. B, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 18 citations in OpenAlex.
- Sequence determinants of the hypomobility of intrinsically disordered proteins in SDS-PAGE.Protein science : a publication of the Protein Society · 2026Article
- Multi-platform quantitation of alpha-synuclein human brain proteoforms suggests disease-specific biochemical profiles of synucleinopathies.Acta neuropathologica communications · 2022Article
- Time-resolved detection of SDS-induced conformational changes in α-synuclein by a micro-stopped-flow system.RSC advances · 2020Article
- A novel method for constructing continuous intrinsic surfaces of nanoparticles.Journal of molecular modeling · 2017Article
- Conformational Ensembles of α-Synuclein Derived Peptide with Different Osmolytes from Temperature Replica Exchange Sampling.Frontiers in neuroscience · 2017Article
- Lysophospholipid-containing membranes modulate the fibril formation of the repeat domain of a human functional amyloid, pmel17.Journal of molecular biology · 2014Article
- Multiscale molecular dynamics simulations of sodium dodecyl sulfate micelles: from coarse-grained to all-atom resolution.Journal of molecular modeling · 2014Article
- Insight into α-synuclein plasticity and misfolding from differential micelle binding.The journal of physical chemistry. B · 2013Article
- Deducing conformational variability of intrinsically disordered proteins from infrared spectroscopy with Bayesian statistics.Chemical physics · 2013Article
- Identification of minimally interacting modules in an intrinsically disordered protein.Biophysical journal · 2012Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
To better understand the interaction of α-synuclein (αSyn) with lipid membranes, we carried out self-assembly molecular dynamics simulations of αSyn with monomeric and micellar sodium dodecyl sulfate (SDS), a widely used membrane mimic. We find that both electrostatic and hydrophobic forces contribute to the interactions of αSyn with SDS. In the presence of αSyn, our simulations suggest that SDS aggregates along the protein chain and forms small-size micelles at very early times. Aggregation is followed by formation of a collapsed protein-SDS micelle complex, which is consistent with experimental results. Finally, interaction of αSyn with preformed micelles induces alterations in the shape of the micelle, and the N-terminal helix (residues 3 through 37) tends to associate with micelles. Overall, our simulations provide an atomistic description of the early time scale αSyn-SDS interaction during the self-assembly of SDS into micelles.
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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.