ArticleThe Journal of biological chemistry2014
The peculiar role of the A2V mutation in amyloid-β (Aβ) 1-42 molecular assembly.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 58 citations in OpenAlex.
- Human iPSC-derived cerebral organoids reveal oxytocin-mediated protection against amyloid-β pathology.Regenerative therapy · 2025Article
- A turn for the worse: Aβ β-hairpins in Alzheimer's disease.Bioorganic & medicinal chemistry · 2024Review
- Aβ1-6Molecular psychiatry · 2023Article
- The interaction of peptide inhibitors and Aβ protein: Binding mode analysis, inhibition of the formation of Aβ aggregates, and then exert neuroprotective effects.Frontiers in aging neuroscience · 2023Article
- A novel bio-inspired strategy to prevent amyloidogenesis and synaptic damage in Alzheimer's disease.Molecular psychiatry · 2022Article
- Dynamics of Amyloid Formation from Simplified Representation to Atomistic Simulations.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Mutations of beta-amyloid precursor protein alter the consequence of Alzheimer's disease pathogenesis.Neural regeneration research · 2019Article
- Oligomers Are Promising Targets for Drug Development in the Treatment of Proteinopathies.Frontiers in molecular neuroscience · 2019Article
- Cu and Zn coordination to amyloid peptides: From fascinating chemistry to debated pathological relevance.Coordination chemistry reviews · 2018Article
- Elucidating the Inhibitory Potential of Designed Peptides Against Amyloid Fibrillation and Amyloid Associated Cytotoxicity.Frontiers in chemistry · 2018Article
- Translational Research in Alzheimer's and Prion Diseases.Journal of Alzheimer's disease : JAD · 2018Review
- HIV-1 matrix protein p17 misfolding forms toxic amyloidogenic assemblies that induce neurocognitive disorders.Scientific reports · 2017Article
- Emergence of Alternative Structures in Amyloid Beta 1-42 Monomeric Landscape by N-terminal Hexapeptide Amyloid Inhibitors.Scientific reports · 2017Article
- The A2V mutation as a new tool for hindering Aβ aggregation: A neutron and x-ray diffraction study.Scientific reports · 2017Article
- High-Resolution Structures of the Amyloid-β 1-42 Dimers from the Comparison of Four Atomistic Force Fields.The journal of physical chemistry. B · 2017Article
- Pyroglutamate-Modified Amyloid-β(3-42) Shows α-Helical Intermediates before Amyloid Formation.Biophysical journal · 2017Article
- The Tat-Aβ1-6A2V(D) peptide against AD synaptopathy.Oncotarget · 2017Article
- Alzheimer's amyloid-β A2T variant and its N-terminal peptides inhibit amyloid-β fibrillization and rescue the induced cytotoxicity.PloS one · 2017Article
- Protein folding, misfolding and aggregation: The importance of two-electron stabilizing interactions.PloS one · 2017Article
- Alternative Selection of β-Site APP-Cleaving Enzyme 1 (BACE1) Cleavage Sites in Amyloid β-Protein Precursor (APP) Harboring Protective and Pathogenic Mutations within the Aβ Sequence.The Journal of biological chemistry · 2016Article
Corrections and comments
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Authors and funding
11 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We recently reported a novel Aβ precursor protein mutation (A673V), corresponding to position 2 of Aβ1-42 peptides (Aβ1-42A2V), that caused an early onset AD-type dementia in a homozygous individual. The heterozygous relatives were not affected as an indication of autosomal recessive inheritance of this mutation. We investigated the folding kinetics of native unfolded Aβ1-42A2V in comparison with the wild type sequence (Aβ1-42WT) and the equimolar solution of both peptides (Aβ1-42MIX) to characterize the oligomers that are produced in the early phases. We carried out the structural characterization of the three preparations using electron and atomic force microscopy, fluorescence emission, and x-ray diffraction and described the soluble oligomer formation kinetics by laser light scattering. The mutation promoted a peculiar pathway of oligomerization, forming a connected system similar to a polymer network with hydrophobic residues on the external surface. Aβ1-42MIX generated assemblies very similar to those produced by Aβ1-42WT, albeit with slower kinetics due to the difficulties of Aβ1-42WT and Aβ1-42A2V peptides in building up of stable intermolecular interaction.
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