ArticleThe Journal of biological chemistry2012
Solid-support electron paramagnetic resonance (EPR) studies of Aβ40 monomers reveal a structured state with three ordered segments.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Alleviating the unwanted effects of oxidative stress on Aβ clearance: a review of related concepts and strategies for the development of computational modelling.Translational neurodegeneration · 2023Review
- Differences in the free energies between the excited states of AProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Is the Conformational Ensemble of Alzheimer's Aβ10-40 Peptide Force Field Dependent?PLoS computational biology · 2017Article
- Interaction of the amyloid β peptide with sodium dodecyl sulfate as a membrane-mimicking detergent.Journal of biological physics · 2016Article
- Amyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.Chemical reviews · 2015Review
- Structural insights into Aβ42 oligomers using site-directed spin labeling.The Journal of biological chemistry · 2013Article
- Thermodynamically stable amyloid-β monomers have much lower membrane affinity than the small oligomers.Frontiers in physiology · 2013Article
- Prion domain of yeast Ure2 protein adopts a completely disordered structure: a solid-support EPR study.PloS one · 2012Article
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Authors and funding
3 authors.
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Abstract
Alzheimer disease is associated with the pathological accumulation of amyloid-β peptide (Aβ) in the brain. Soluble Aβ oligomers formed during early aggregation process are believed to be neurotoxins and causative agents in Alzheimer disease. Aβ monomer is the building block for amyloid assemblies. A comprehensive understanding of the structural features of Aβ monomer is crucial for delineating the mechanism of Aβ oligomerization. Here we investigated the structures of Aβ40 monomer using a solid-support approach, in which Aβ40 monomers are tethered on the solid support via an N-terminal His tag to prevent further aggregation. EPR spectra of tethered Aβ40 with spin labels at 18 different positions show that Aβ40 monomers adopt a completely disordered structure under denaturing conditions. Under native conditions, however, EPR spectra suggest that Aβ40 monomers adopt both a disordered state and a structured state. The structured state of Aβ40 monomer has three more ordered segments at 14-18, 29-30, and 38-40. Interactions between these segments may stabilize the structured state, which likely plays an important role in Aβ aggregation.
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