ArticleBiophysical journal2007
Structure and dynamics of parallel beta-sheets, hydrophobic core, and loops in Alzheimer's A beta fibrils.
Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
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Who cites it
56 citing papers in PubMed.
- Bioinformatic assessment of the potential amyloidogenicity of the human and evolutionarily more ancient proteomes.The Biochemical journal · 2026Article
- Multiscale Simulations Elucidate the Mechanism of Polyglutamine Aggregation and the Role of Flanking Domains in Fibril Polymorphism.The journal of physical chemistry. B · 2025Article
- Efficient and accurate binding free energy calculation of AβProteins · 2025Article
- Multiscale simulations elucidate the mechanism of polyglutamine aggregation and the role of flanking domains in fibril polymorphism.bioRxiv : the preprint server for biology · 2025Article
- Targeting multiple pathways with virtual screening to identify the multi-target agent for Alzheimer's disease treatment.Journal of computer-aided molecular design · 2025Article
- Bridging prion biology and Alzheimer's disease: from pathogenic seeds to precision therapeutics.Frontiers in molecular neuroscience · 2025Review
- An N-terminal acidic β-sheet domain is responsible for the metal-accumulation properties of amyloid-β protofibrils: a molecular dynamics study.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2024Article
- Genetic architecture of hippocampus subfields volumes in Alzheimer's disease.CNS neuroscience & therapeutics · 2024Article
- Molecular dynamics study of water channels in natural and synthetic amyloid-β fibrils.The Journal of chemical physics · 2021Article
- Curcumin as Scaffold for Drug Discovery against Neurodegenerative Diseases.Biomedicines · 2021Review
- Structure and Function of Alzheimer's Amyloid βeta Proteins from Monomer to Fibrils: A Mini Review.The protein journal · 2019Review
- Amyloid Fibril Design: Limiting Structural Polymorphism in Alzheimer's Aβ Protofilaments.The journal of physical chemistry. B · 2018Article
- Structural Modulation of Human Amylin Protofilaments by Naturally Occurring Mutations.The journal of physical chemistry. B · 2018Article
- Energetics Underlying Twist Polymorphisms in Amyloid Fibrils.The journal of physical chemistry. B · 2018Article
- Elongation affinity, activation barrier, and stability of Aβ42 oligomers/fibrils in physiological saline.Biochemical and biophysical research communications · 2017Article
- Role of the N-terminus for the stability of an amyloid-β fibril with three-fold symmetry.PloS one · 2017Article
- Structural and fluctuational difference between two ends of Aβ amyloid fibril: MD simulations predict only one end has open conformations.Scientific reports · 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
- Membrane Protein Structure, Function, and Dynamics: a Perspective from Experiments and Theory.The Journal of membrane biology · 2015Review
- On the lack of polymorphism in Aβ-peptide aggregates derived from patient brains.Protein science : a publication of the Protein Society · 2015Article
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2 authors.
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Abstract
We explore the relative contributions of different structural elements to the stability of Abeta fibrils by molecular-dynamics simulations performed over a broad range of temperatures (298 K to 398 K). Our fibril structures are based on solid-state nuclear magnetic resonance experiments of Abeta(1-40) peptides, with sheets of parallel beta-strands connected by loops and stabilized by interior salt bridges. We consider models with different interpeptide interfaces, and different staggering of the N- and C-terminal beta-strands along the fibril axis. Multiple 10-20 ns molecular-dynamics simulations show that fibril segments with 12 peptides are stable at ambient temperature. The different models converge toward an interdigitated side-chain packing, and present water channels solvating the interior D23/K28 salt bridges. At elevated temperatures, we observe the early phases of fibril dissociation as a loss of order in the hydrophilic loops connecting the two beta-strands, and in the solvent-exposed N-terminal beta-sheets. As the most dramatic structural change, we observe collective sliding of the N- and C-terminal beta-sheets on top of each other. The interior C-terminal beta-sheets in the hydrophobic core remain largely intact, indicating that their formation and stability is crucial to the dissociation/elongation and stability of Abeta fibrils.
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