ArticleProteins2010
A molecular dynamics study of the early stages of amyloid-beta(1-42) oligomerization: the role of lipid membranes.
Article in Proteins, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
What it found
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Who cites it
27 citing papers in PubMed.
- The Influence of POPC as a Coaggregate in Amyloid-β Oligomer Formation.ACS chemical neuroscience · 2025Article
- Calcium inhibits penetration of Alzheimer's AβProteins · 2022Article
- Molecular insights into the primary nucleation of polymorphic amyloid β dimers in DOPC lipid bilayer membrane.Protein science : a publication of the Protein Society · 2022Article
- An Overview of Several Inhibitors for Alzheimer's Disease: Characterization and Failure.International journal of molecular sciences · 2021Review
- Promising tacrine/huperzine A-based dimeric acetylcholinesterase inhibitors for neurodegenerative disorders: From relieving symptoms to modifying diseases through multitarget.Journal of neurochemistry · 2021Review
- Defining the Neuropathological Aggresome acrossThe journal of physical chemistry. B · 2021Review
- The membrane axis of Alzheimer's nanomedicine.Advanced nanobiomed research · 2021Article
- Review
- Modelling of interactions between Aβ(25-35) peptide and phospholipid bilayers: effects of cholesterol and lipid saturation.RSC advances · 2020Article
- Effect of lipid saturation on amyloid-beta peptide partitioning and aggregation in neuronal membranes: molecular dynamics simulations.European biophysics journal : EBJ · 2019Article
- Characterization of Lipid-Protein Interactions and Lipid-Mediated Modulation of Membrane Protein Function through Molecular Simulation.Chemical reviews · 2019Review
- Concentration-dependent effects of mercury and lead on Aβ42: possible implications for Alzheimer's disease.European biophysics journal : EBJ · 2019Article
- Physical determinants of the self-replication of protein fibrils.Nature physics · 2016Article
- Maximally asymmetric transbilayer distribution of anionic lipids alters the structure and interaction with lipids of an amyloidogenic protein dimer bound to the membrane surface.Chemistry and physics of lipids · 2016Article
- Lipid insertion domain unfolding regulates protein orientational transition behavior in a lipid bilayer.Biophysical chemistry · 2015Article
- Amyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.Chemical reviews · 2015Review
- Scaling and alpha-helix regulation of protein relaxation in a lipid bilayer.The Journal of chemical physics · 2014Article
- Structural diversity of Alzheimer's disease amyloid-β dimers and their role in oligomerization and fibril formation.Journal of Alzheimer's disease : JAD · 2014Article
- Molecular interactions of Alzheimer amyloid-β oligomers with neutral and negatively charged lipid bilayers.Physical chemistry chemical physics : PCCP · 2013Article
- Mechanisms for the Insertion of Toxic, Fibril-like β-Amyloid Oligomers into the Membrane.Journal of chemical theory and computation · 2013Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
As research progresses toward understanding the role of the amyloid-beta (Abeta) peptide in Alzheimer's disease, certain aspects of the aggregation process for Abeta are still not clear. In particular, the accepted constitution of toxic aggregates in neurons has shifted toward small oligomers. However, the process of forming these oligomers in cells is also not full clear. Even more interestingly, it has been implied that cell membranes, and, in particular, anionic lipids within those membranes, play a key role in the progression of Abeta aggregation, but the exact nature of the Abeta-membrane interaction in this process is unknown. In this work, we use a thermodynamic cycle and umbrella sampling molecular dynamics to investigate dimerization of the 42-residue Abeta peptide on model zwitterionic dipalmitoylphosphatidylcholine (DPPC) or model anionic dioleoylphosphatidylserine (DOPS) bilayer surfaces. We determined that Abeta dimerization was strongly favored through interactions with the DOPS bilayer. Further, our calculations showed that the DOPS bilayer promoted strong protein-protein interactions within the Abeta dimer, whereas DPPC favored strong protein-lipid interactions. By promoting dimer formation and subsequent dimer release into the solvent, the DOPS bilayer acts as a catalyst in Abeta aggregation.
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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.