ArticleBiochemical and biophysical research communications2021
Alzheimer's Aβ42 and Aβ40 form mixed oligomers with direct molecular interactions.
Article in Biochemical and biophysical research communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Targeting the BACE1-GSK-3β Signaling Axis in Alzheimer's Disease: From Molecular Crosstalk to Nanotechnology-Based Translational Strategies.Molecular neurobiology · 2026Review
- In vitro, cellular and in vivo studies of amyloid oligomers structure and toxicity: Challenges and advances.Protein science : a publication of the Protein Society · 2026Review
- Differentiating Alzheimer's Aβ Isoforms Coaggregated in Cerebrospinal Fluid via Single-Particle Imaging.ACS chemical neuroscience · 2026Article
- Uncovering Amyloid-β Interactions: Gray versus White Matter.ACS chemical neuroscience · 2025Article
- Newer Therapeutic Approaches in Treating Alzheimer's Disease: A Comprehensive Review.ACS omega · 2025Review
- Pathological Mechanisms and Molecular Imaging Advances in Alzheimer's Disease.Clinical interventions in aging · 2025Review
- Survey of the Aβ-peptide structural diversity: molecular dynamics approaches.Biophysical reviews · 2024Review
- Inhibiting mtDNA-STING-NLRP3/IL-1β axis-mediated neutrophil infiltration protects neurons in Alzheimer's disease.Cell proliferation · 2024Article
- Heterotypic Interactions between the 40- and 42-Residue Isoforms of β-Amyloid Peptides on Lipid Bilayer Surfaces.ACS chemical neuroscience · 2023Article
- Article
- Exploring the Role of Glycolytic Enzymes PFKFB3 and GAPDH in the Modulation of Aβ and Neurodegeneration and Their Potential of Therapeutic Targets in Alzheimer's Disease.Applied biochemistry and biotechnology · 2023Review
- Aβ40 Aggregation under Changeable Conditions.International journal of molecular sciences · 2023Article
- Design and Synthesis of 6-O-Phosphorylated Heparan Sulfate Oligosaccharides to Inhibit Amyloid β Aggregation.Chembiochem : a European journal of chemical biology · 2022Article
- Location of the cross-β structure in prion fibrils: A search by seeding and electron spin resonance spectroscopy.Protein science : a publication of the Protein Society · 2022Article
- Sticker-and-spacer model for amyloid beta condensation and fibrillation.Frontiers in molecular neuroscience · 2022Article
- A Multi-Chamber Paper-Based Platform for the Detection of Amyloid β Oligomers 42 via Copper-Enhanced Gold Immunoblotting.Biomolecules · 2021Article
- Lipid membranes induce structural conversion from amyloid oligomers to fibrils.Biochemical and biophysical research communications · 2021Article
- Effect of spin labelling on the aggregation kinetics of yeast prion protein Ure2.Royal Society open science · 2021Article
- The Common Alzheimer's Disease Research Ontology (CADRO) for biomarker categorization.Alzheimer's & dementia (New York, N. Y.)Review
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2 authors.
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Abstract
Formation of Aβ oligomers and fibrils plays a central role in the pathogenesis of Alzheimer's disease. There are two major forms of Aβ in the brain: Aβ42 and Aβ40. Aβ42 is the major component of the amyloid plaques, but the overall abundance of Aβ40 is several times that of Aβ42. In vitro experiments show that Aβ42 and Aβ40 affect each other's aggregation. In mouse models of Alzheimer's disease, overexpression of Aβ40 has been shown to reduce the plaque pathology, suggesting that Aβ42 and Aβ40 also interact in vivo. Here we address the question of whether Aβ42 and Aβ40 interact with each other in the formation of oligomers using electron paramagnetic resonance (EPR) spectroscopy. When the Aβ42 oligomers were formed using only spin-labeled Aβ42, the dipolar interaction between spin labels that are within 20 Å range broadened the EPR spectrum and reduced its amplitude. Oligomers formed with a mixture of spin-labeled Aβ42 and wild-type Aβ42 gave an EPR spectrum with higher amplitude due to weakened spin-spin interactions, suggesting molecular mixing of labeled and wild-type Aβ42. When spin-labeled Aβ42 and wild-type Aβ40 were mixed to form oligomers, the resulting EPR spectrum also showed reduced amplitude, suggesting that wild-type Aβ40 can also form oligomers with spin-labeled Aβ42. Therefore, our results suggest that Aβ42 and Aβ40 form mixed oligomers with direct molecular interactions. Our results point to the importance of investigating Aβ42-Aβ40 interactions in the brain for a complete understanding of Alzheimer's pathogenesis and therapeutic interventions.
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