ArticleBiophysical journal2010
Retardation of Abeta fibril formation by phospholipid vesicles depends on membrane phase behavior.
Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 74 citations in OpenAlex.
- Multimodal MRI Reveals Cerebral and Vascular Amyloid-Driven Myeloarchitectural Disorganization in a Mouse Model of Alzheimer's Disease.NMR in biomedicine · 2026Article
- Combinations of Vitamin A and Vitamin E Metabolites Confer Resilience against Amyloid-β Aggregation.ACS chemical neuroscience · 2023Article
- A Kinetic Map of the Influence of Biomimetic Lipid Model Membranes on AβACS chemical neuroscience · 2023Article
- Tuning the surface charge of phospholipid bilayers inhibits insulin fibrilization.Colloids and surfaces. B, Biointerfaces · 2022Article
- The amyloid-inhibiting NCAM-PrP peptide targets Aβ peptide aggregation in membrane-mimetic environments.iScience · 2021Article
- Lipid membranes induce structural conversion from amyloid oligomers to fibrils.Biochemical and biophysical research communications · 2021Article
- Defining the Neuropathological Aggresome acrossThe journal of physical chemistry. B · 2021Review
- A dopamine metabolite stabilizes neurotoxic amyloid-β oligomers.Communications biology · 2021Article
- Mixed Phospholipid Vesicles Catalytically Inhibit and Reverse Amyloid Fibril Formation.The journal of physical chemistry letters · 2020Article
- Fibrillization of 40-Residue β-Amyloid Peptides in Membrane-Like Environments Leads to Different Fibril Structures and Reduced Molecular Polymorphisms.Biomolecules · 2020Article
- Acetylation of AβACS chemical neuroscience · 2020Article
- The on-fibrillation-pathway membrane content leakage and off-fibrillation-pathway lipid mixing induced by 40-residue β-amyloid peptides in biologically relevant model liposomes.Biochimica et biophysica acta. Biomembranes · 2018Article
- Cholesterol catalyses Aβ42 aggregation through a heterogeneous nucleation pathway in the presence of lipid membranes.Nature chemistry · 2018Article
- Increased midlife triglycerides predict brain β-amyloid and tau pathology 20 years later.Neurology · 2018Article
- Article
- Effects of Charged Cholesterol Derivatives on Aβ40 Amyloid Formation.The journal of physical chemistry. B · 2016Article
- On the lag phase in amyloid fibril formation.Physical chemistry chemical physics : PCCP · 2015Review
- Amyloid fibrillation of insulin under water-limited conditions.Biophysical journal · 2014Article
- Charge dependent retardation of amyloid β aggregation by hydrophilic proteins.ACS chemical neuroscience · 2014Article
- Biochemistry of amyloid β-protein and amyloid deposits in Alzheimer disease.Cold Spring Harbor perspectives in medicine · 2012Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
An increasing amount of evidence suggests that in several amyloid diseases, the fibril formation in vivo and the mechanism of toxicity both involve membrane interactions. We have studied Alzheimer's disease related amyloid beta peptide (Abeta). Recombinant Abeta(M1-40) and Abeta(M1-42) produced in Escherichia coli, allows us to carry out large scale kinetics assays with good statistics. The amyloid formation process is followed in means of thioflavin T fluorescence at relatively low (down to 380 nM) peptide concentration approaching the physiological range. The lipid membranes are introduced in the system as large and small unilamellar vesicles. The aggregation lagtime increases in the presence of lipid vesicles for all situations investigated and the phase behavior of the membrane in the vesicles has a large effect on the aggregation kinetics. By comparing vesicles with different membrane phase behavior we see that the solid gel phase dipalmitoylphosphatidylcholine bilayers cause the largest retardation of Abeta fibril formation. The membrane-induced retardation reaches saturation and is present when the vesicles are added during the lag time up to the nucleation point. No significant difference is detected in lag time when increasing amount of negative charge is incorporated into the membrane.
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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.