ArticleJournal of biological physics2016
Interaction of the amyloid β peptide with sodium dodecyl sulfate as a membrane-mimicking detergent.
Article in Journal of biological physics, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 31 citations in OpenAlex.
- Increase of brain Aβ peptides and secretase activity during normal aging in rodent and human.GeroScience · 2026Article
- The influence of a dicationic surfactant on the aggregation process of the IVAGVN peptide derived from the human cystatin C sequence (56-61).RSC advances · 2025Article
- Air pollution amyloidogenesis is attenuated by the gamma-secretase modulator GSM-15606.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2024Article
- Amyloid futures in the expanding pathology of brain aging and dementia.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2023Article
- Molecular Mechanisms of Inhibition of Protein Amyloid Fibril Formation: Evidence and Perspectives Based on Kinetic Models.International journal of molecular sciences · 2022Review
- Inducible fold-switching as a mechanism to fibrillate pro-apoptotic BCL-2 proteins.Biopolymers · 2021Article
- The membrane axis of Alzheimer's nanomedicine.Advanced nanobiomed research · 2021Article
- In situ kinetic measurements of α-synuclein aggregation reveal large population of short-lived oligomers.PloS one · 2021Article
- Humanin selectively prevents the activation of pro-apoptotic protein BID by sequestering it into fibers.The Journal of biological chemistry · 2020Article
- Long-range Regulation of Partially Folded Amyloidogenic Peptides.Scientific reports · 2020Article
- A Capped Peptide of the Aggregation Prone NAC 71-82 Amino Acid Stretch of α-Synuclein Folds into Soluble β-Sheet Oligomers at Low and Elevated Peptide Concentrations.International journal of molecular sciences · 2020Article
- Impact of membrane curvature on amyloid aggregation.Biochimica et biophysica acta. Biomembranes · 2018Review
- Protein folding, misfolding and aggregation: The importance of two-electron stabilizing interactions.PloS one · 2017Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The amyloid β (A β) peptide is important in the context of Alzheimer's disease, since it is one of the major components of the fibrils that constitute amyloid plaques. Agents that can influence fibril formation are important, and of those, membrane mimics are particularly relevant, because the hydrophobic part of A β suggests a possible membrane activity of the peptide. We employed spin-label EPR to investigate the aggregation process of A β1-40 in the presence of the sodium dodecyl sulfate (SDS) detergent as a membrane-mimicking agent. In this work, the effect of SDS on A β is studied using two positions of spin label, the N-terminus and position 26. By comparing the two label positions, the effect of local mobility of the spin label is eliminated, revealing A β aggregation in the SDS concentration regime below the critical micelle concentration (CMC). We demonstrate that, at low SDS concentrations, the N-terminus of A β participates in the solubilization, most likely by being located at the particle-water interface. At higher SDS concentrations, an SDS-solubilized state that is a precursor to the one A β/micelle state above the CMC of SDS prevails. We propose that A β is membrane active and that aggregates include SDS. This study reveals the unique potential of EPR in studying A β aggregation in the presence of detergent.
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