ArticleBiophysical journal2012
Binding of β-amyloid (1-42) peptide to negatively charged phospholipid membranes in the liquid-ordered state: modeling and experimental studies.
Article in Biophysical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 96 citations in OpenAlex.
- Amyloid Protein-Induced Remodeling of Morphometry and Nanomechanics in Human Platelets.Biomedicines · 2025Article
- Amyloid β Peptide Modifies Membrane Architecture and Surface Electrostatic Properties of Human Red Blood Cells.International journal of molecular sciences · 2025Article
- Transient cholesterol interactions with the amyloid precursor protein involved in Alzheimer's disease pathogenesis.Biophysical reviews · 2025Review
- Aromatic Anion Carrier via Self-Assembly with Imidazolium-Fused Aromatic Amphiphiles.Precision chemistry · 2025Article
- Diverse Interactions of Sterols with Amyloid Precursor Protein Transmembrane Domain Can Shift Distribution Between Alternative Amyloid-β Production Cascades in Manner Dependent on Local Lipid Environment.International journal of molecular sciences · 2025Article
- Understanding Aβ Peptide Binding to Lipid Membranes: A Biophysical Perspective.International journal of molecular sciences · 2024Review
- The Influence of Lipid Electric Charge on the Binding of Aβ(1-42) Amyloid Peptide to Bilayers in the Liquid-Ordered State.Biomolecules · 2024Article
- Heterotypic Interactions between the 40- and 42-Residue Isoforms of β-Amyloid Peptides on Lipid Bilayer Surfaces.ACS chemical neuroscience · 2023Article
- Amyposomes, a nanotechnological chaperone with anti-amyloidogenic activity.Annals of medicine · 2023Article
- LILRB2-mediated TREM2 signaling inhibition suppresses microglia functions.Molecular neurodegeneration · 2022Article
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- Neuroinflammatory Signaling in the Pathogenesis of Alzheimer's Disease.Current neuropharmacology · 2022Review
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- Melatonin: Regulation of Biomolecular Condensates in Neurodegenerative Disorders.Antioxidants (Basel, Switzerland) · 2021Review
- Cryo-electron Microscopy Imaging of Alzheimer's Amyloid-beta 42 Oligomer Displayed on a Functionally and Structurally Relevant Scaffold.Angewandte Chemie (International ed. in English) · 2021Article
- Mechanisms and therapeutic potential of interactions between human amyloids and viruses.Cellular and molecular life sciences : CMLS · 2021Review
- Toxic oligomers of the amyloidogenic HypF-N protein form pores in mitochondrial membranes.Scientific reports · 2020Article
- Anti-aggregation Effects of Phenolic Compounds on α-synuclein.Molecules (Basel, Switzerland) · 2020Review
- Mitochondria as intracellular signaling platforms in health and disease.The Journal of cell biology · 2020Review
- The Binding of Aβ42 Peptide Monomers to Sphingomyelin/Cholesterol/Ganglioside Bilayers Assayed by Density Gradient Ultracentrifugation.International journal of molecular sciences · 2020Article
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Authors and funding
8 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
To explore the initial stages of amyloid β peptide (Aβ42) deposition on membranes, we have studied the interaction of Aβ42 in the monomeric form with lipid monolayers and with bilayers in either the liquid-disordered or the liquid-ordered (L(o)) state, containing negatively charged phospholipids. Molecular dynamics (MD) simulations of the system have been performed, as well as experimental measurements. For bilayers in the L(o) state, in the absence of the negatively charged lipids, interaction is weak and it cannot be detected by isothermal calorimetry. However, in the presence of phosphatidic acid, or of cardiolipin, interaction is detected by different methods and in all cases interaction is strongest with lower (2.5-5 mol%) than higher (10-20 mol%) proportions of negatively charged phospholipids. Liquid-disordered bilayers consistently allowed a higher Aβ42 binding than L(o) ones. Thioflavin T assays and infrared spectroscopy confirmed a higher proportion of β-sheet formation under conditions when higher peptide binding was measured. The experimental results were supported by MD simulations. We used 100 ns MD to examine interactions between Aβ42 and three different 512 lipid bilayers consisting of palmitoylsphingomyelin, dimyristoyl phosphatidic acid, and cholesterol in three different proportions. MD pictures are different for the low- and high-charge bilayers, in the former case the peptide is bound through many contact points to the bilayer, whereas for the bilayer containing 20 mol% anionic phospholipid only a small fragment of the peptide appears to be bound. The MD results indicate that the binding and fibril formation on the membrane surface depends on the composition of the bilayer, and is the result of a subtle balance of many inter- and intramolecular interactions between the Aβ42 and membrane.
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