ArticleBiochemistry2011
Single-molecule atomic force microscopy force spectroscopy study of Aβ-40 interactions.
Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed.
- Applying the Atomic Force Microscopy Technique in Medical Sciences-A Narrative Review.Biomedicines · 2024Review
- A turn for the worse: Aβ β-hairpins in Alzheimer's disease.Bioorganic & medicinal chemistry · 2024Review
- Multivariate effects of pH, salt, and ZnCommunications chemistry · 2022Article
- Visualizing and trapping transient oligomers in amyloid assembly pathways.Biophysical chemistry · 2021Review
- Mechanical Stability of a Small, Highly-Luminescent Engineered Protein NanoLuc.International journal of molecular sciences · 2020Article
- The CAR T-Cell Mechanoimmunology at a Glance.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2020Review
- AFM Probing of Amyloid-Beta 42 Dimers and Trimers.Frontiers in molecular biosciences · 2020Article
- Spontaneous self-assembly of amyloid β (1-40) into dimers.Nanoscale advances · 2019Article
- Probing the Basis of α-Synuclein Aggregation by Comparing Simulations to Single-Molecule Experiments.Biophysical journal · 2019Article
- Force clamp approach for characterization of nano-assembly in amyloid beta 42 dimer.Nanoscale · 2019Article
- Probing Intermolecular Interactions within the Amyloid β Trimer Using a Tethered Polymer Nanoarray.Bioconjugate chemistry · 2018Article
- A peptide-display protein scaffold to facilitate single molecule force studies of aggregation-prone peptides.Protein science : a publication of the Protein Society · 2018Article
- Friction Determination by Atomic Force Microscopy in Field of Biochemical Science.Micromachines · 2018Review
- Improving estimation of kinetic parameters in dynamic force spectroscopy using cluster analysis.The Journal of chemical physics · 2018Article
- APP/Aβ structural diversity and Alzheimer's disease pathogenesis.Neurochemistry international · 2017Review
- Single-molecule probing of amyloid nano-ensembles using the polymer nanoarray approach.Physical chemistry chemical physics : PCCP · 2017Article
- Nano-assembly of amyloid β peptide: role of the hairpin fold.Scientific reports · 2017Article
- Monomer Dynamics of Alzheimer Peptides and Kinetic Control of Early Aggregation in Alzheimer's Disease.Chemphyschem : a European journal of chemical physics and physical chemistry · 2016Article
- Effect of acidic pH on the stability of α-synuclein dimers.Biopolymers · 2016Article
- Copper-induced structural conversion templates prion protein oligomerization and neurotoxicity.Science advances · 2016Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Misfolding and aggregation of amyloid β-40 (Aβ-40) peptide play key roles in the development of Alzheimer's disease (AD). However, very little is known about the molecular mechanisms underlying these molecular processes. We developed a novel experimental approach that can directly probe aggregation-prone states of proteins and their interactions. In this approach, the proteins are anchored to the surface of the atomic force microscopy substrate (mica) and the probe, and the interaction between anchored molecules is measured in the approach-retraction cycles. We used dynamic force spectroscopy (DFS) to measure the stability of transiently formed dimers. One of the major findings from DFS analysis of α-synuclein (α-Syn) is that dimeric complexes formed by misfolded α-Syn protein are very stable and dissociate over a range of seconds. This differs markedly from the dynamics of monomers, which occurs on a microsecond to nanosecond time scale. Here we applied the same approach to quantitatively characterize interactions of Aβ-40 peptides over a broad range of pH values. These studies showed that misfolded dimers are characterized by lifetimes in the range of seconds. This value depends on pH and varies between 2.7 s for pH 2.7 and 0.1 s for pH 7, indicating that the aggregation properties of Aβ-40 are modulated by the environmental conditions. The analysis of the contour lengths revealed the existence of various pathways for dimer dissociation, suggesting that dimers with different conformations are formed. These structural variations result in different aggregation pathways, leading to different types of oligomers and higher-order aggregates, including fibrils.
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Registered trials
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