ArticleNanomedicine : nanotechnology, biology, and medicine2014
Nanoprobing of misfolding and interactions of amyloid β 42 protein.
Article in Nanomedicine : nanotechnology, biology, and medicine, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Targeting soluble misfolded oligomers in anti-amyloid research.Nature reviews. Chemistry · 2026Review
- Structural biology of cell surface receptors implicated in Alzheimer's disease.Biophysical reviews · 2022Review
- Visualizing and trapping transient oligomers in amyloid assembly pathways.Biophysical chemistry · 2021Review
- 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
- Force clamp approach for characterization of nano-assembly in amyloid beta 42 dimer.Nanoscale · 2019Article
- Self-assembly of the full-length amyloid Aβ42 protein in dimers.Nanoscale · 2016Article
- 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
- Probing of Amyloid Aβ (14-23) Trimers by Single-Molecule Force Spectroscopy.Jacobs journal of molecular and translational medicine · 2016Article
- Amyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.Chemical reviews · 2015Review
- Direct Detection of α-Synuclein Dimerization Dynamics: Single-Molecule Fluorescence Analysis.Biophysical journal · 2015Article
- Amyloid misfolding, aggregation, and the early onset of protein deposition diseases: insights from AFM experiments and computational analyses.AIMS molecular science · 2015Article
- The structure of misfolded amyloidogenic dimers: computational analysis of force spectroscopy data.Biophysical journal · 2014Article
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Authors and funding
2 authors.
Funding
Abstract
The assembly of amyloid β (Aβ) proteins into nanostructures is currently considered a major pathway of Alzheimer's disease development, but the molecular mechanisms of this self-assembly process remains unclear. Recently, we showed that single-molecule AFM force spectroscopy (SMFS) is capable of probing the dynamics and interaction between Aβ40 peptides, and these studies allowed us to shed new light on transiently existing Aβ40 misfolding states. In this study, we applied the same SMFS approach to characterize the misfolding of Aβ42 peptide, the most toxic Aβ alloform. The quantitative analysis of SMFS data demonstrated that Aβ interaction leads to the formation of dimers with a lifetime in the range of a second. Interaction via C-terminal segments prevailed at pH 7, but interaction within the peptide center prevailed at acidic pH levels. The difference in the misfolding properties for Aβ40 and Aβ42 peptides and the mechanisms of amyloid nanoassembly are discussed. FROM THE CLINICAL EDITOR: Despite decades of intense research, Alzheimer's disease still remains incurable. This novel study focuses on the assembly of amyloid β proteins into nanostructures, which is a key mechanism in Alzheimer's disease development. Single molecule atomic force spectroscopy is utilized to shed light on the molecular mechanisms of this self-assembly process.
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