ArticleThe journal of physical chemistry. B2013
Molecular mechanism of misfolding and aggregation of Aβ(13-23).
Article in The journal of physical chemistry. B, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
What it found
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Who cites it
26 citing papers in PubMed, 48 citations in OpenAlex.
- Denaturation of firefly luciferase at heat shock temperatures captured in silico.Biophysical journal · 2025Article
- Applying the Atomic Force Microscopy Technique in Medical Sciences-A Narrative Review.Biomedicines · 2024Review
- Computational screening for new neuroprotective ingredients against Alzheimer's disease from bilberry by cheminformatics approaches.Frontiers in nutrition · 2022Article
- Piecewise All-Atom SMD Simulations Reveal Key Secondary Structures in Luciferase Unfolding Pathway.Biophysical journal · 2020Article
- Two C-terminal sequence variations determine differential neurotoxicity between human and mouse α-synuclein.Molecular neurodegeneration · 2020Article
- 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
- Probing Intermolecular Interactions within the Amyloid β Trimer Using a Tethered Polymer Nanoarray.Bioconjugate chemistry · 2018Article
- Strikingly different effects of cholesterol and 7-ketocholesterol on lipid bilayer-mediated aggregation of amyloid beta (1-42).Biochemistry and biophysics reports · 2018Article
- Friction Determination by Atomic Force Microscopy in Field of Biochemical Science.Micromachines · 2018Review
- Nanoscale Dynamics of Amyloid β-42 Oligomers As Revealed by High-Speed Atomic Force Microscopy.ACS nano · 2017Article
- 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
- A novel pathway for amyloids self-assembly in aggregates at nanomolar concentration mediated by the interaction with surfaces.Scientific reports · 2017Article
- Self-assembly of the full-length amyloid Aβ42 protein in dimers.Nanoscale · 2016Article
- Probing of Amyloid Aβ (14-23) Trimers by Single-Molecule Force Spectroscopy.Jacobs journal of molecular and translational medicine · 2016Article
- A Metal-free Click Chemistry Approach for the Assembly and Probing of Biomolecules.Journal of nature and science · 2016Article
- AFM-Based Single Molecule Techniques: Unraveling the Amyloid Pathogenic Species.Current pharmaceutical design · 2016Review
- A flexible nanoarray approach for the assembly and probing of molecular complexes.Biophysical journal · 2015Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The misfolding and self-assembly of the amyloid-beta (Aβ) peptide into aggregates is a molecular signature of the development of Alzheimer's disease, but molecular mechanisms of the peptide aggregation remain unknown. Here, we combined Atomic Force Microscopy (AFM) and Molecular Dynamics (MD) simulations to characterize the misfolding process of an Aβ peptide. Dynamic force spectroscopy AFM analysis showed that the peptide forms stable dimers with a lifetime of ∼1 s. During MD simulations, isolated monomers gradually adopt essentially similar nonstructured conformations independent from the initial structure. However, when two monomers approach their structure changes dramatically, and the conformational space for the two monomers become restricted. The arrangement of monomers in antiparallel orientation leads to the cooperative formation of β-sheet conformation. Interactions, including hydrogen bonds, salt bridges, and weakly polar interactions of side chains stabilize the structure of the dimer. Under the applied force, the dimer, as during the AFM experiments, dissociates in a cooperative manner. Thus, misfolding of the Aβ peptide proceeds via the loss of conformational flexibility and formation of stable dimers suggesting their key role in the subsequent Aβ aggregation process.
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What OpenQuestion holds
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.