ArticleChemistry and physics of lipids2018
Interaction of the β amyloid - Aβ(25-35) - peptide with zwitterionic and negatively charged vesicles with and without cholesterol.
Article in Chemistry and physics of lipids, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
3 citing papers in PubMed, 7 citations in OpenAlex.
- Interactions of Sucrose and Trehalose with Lysozyme in Different Media: A Perspective from Atomistic Molecular Dynamics Simulations.Molecular pharmaceutics · 2025Article
- Fluorescence in colloidal solutions: Scattering vs physicochemical effects on line shape.Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy · 2023Article
- Modelling of interactions between Aβ(25-35) peptide and phospholipid bilayers: effects of cholesterol and lipid saturation.RSC advances · 2020Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The interactions of the Alzheimer's β-amyloid peptide, Aβ(25-35), with 18:1 (Δ9-Cis) PC 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC), L-α-phosphatidylcholine (EPC), 1,2-dioleoyl-sn-glycero-3-phospho-(1'-rac-glycerol) (sodium salt) (DOPG), and L-α-phosphatidylglycerol (EPG) phospholipid vesicles with and without cholesterol (Ch) are studied by the nitroxide spin probe electron paramagnetic resonance (EPR) method. Two nitroxide spin probes, 2,2,6,6-tetramethyl-piperidin-1-oxyl-4-yl hexadecanoate (TP, TEMPO-Palmitate) and 2-Ethyl-2-(15-methoxy-15-oxopentadecyl)-4,4-dimethyl-3-oxazolidinyloxy (16-DSE), are utilized in the study. TEMPO-Palmitate has the reporting EPR moiety located at the top of this spin probe, while 16-DSE has the reporting EPR moiety located at the tail of the spin probe. These two probes enable us to sample the surface and the middle of the phospholipid bilayer, respectively. All EPR measurements are done above the melting points of all four phospholipids when the bilayer is in the liquid crystal phase, the physiologically relevant phase. Due to non-linear spectral line fitting, the EPR spectral parameters are extracted with high precision. The results show that there are two populations of Aβ(25-35) and that one of them is located in the hydrophobic phospholipid layer below the hydrophilic headgroup region. The second population appears to be weakly coupled to the surface of the bilayer. Both hydrophobic and electrostatic interactions affect the insertion of Aβ(25-35) in the bilayer. Also, there is strong evidence for an interaction between cholesterol and Aβ(25-35), which affects the dielectric and dynamic properties of the bilayer.
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Registered trials
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