ArticleScientific reports2018
Nanostructural Differentiation and Toxicity of Amyloid-β25-35 Aggregates Ensue from Distinct Secondary Conformation.
Article in Scientific reports, 2018. 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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14 citing papers in PubMed, 38 citations in OpenAlex.
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- Free Energy Perturbation Simulations Measure the Change in Binding Affinity of the Aβ25-35 Peptide to the Zwitterionic Bilayer Caused by Oxidation.Journal of chemical information and modeling · 2025Article
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- Moderate aerobic training enhances the effectiveness of insulin therapy through hypothalamic IGF1 signaling in rat model of Alzheimer's disease.Scientific reports · 2024Article
- Effect of the aggregation state of amyloid-beta (25-35) on the brain oxidative stress in vivo.PloS one · 2024Article
- Polyphenol-based polymer nanoparticles for inhibiting amyloid protein aggregation: recent advances and perspectives.Frontiers in nutrition · 2024Review
- Toward determining amyloid fibril structures using experimental constraints from Raman spectroscopy.The Journal of chemical physics · 2023Article
- Protective Effects ofLife (Basel, Switzerland) · 2023Article
- Protein Predictive Modeling and Simulation of Mutations of Presenilin-1 Familial Alzheimer's Disease on the Orthosteric Site.Frontiers in molecular biosciences · 2021Article
- Formation of distinct prion protein amyloid fibrils under identical experimental conditions.Scientific reports · 2020Article
- De novo aggregation of Alzheimer's Aβ25-35 peptides in a lipid bilayer.Scientific reports · 2019Article
- Structure of amyloid βScientific reports · 2019Article
- Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Amyloid nanostructures are originated from protein misfolding and aberrant aggregation, which is associated with the pathogenesis of many types of degenerative diseases, such as Alzheimer's disease (AD), Parkinson's disease (PD) and Huntington's disease. The secondary conformation of peptides is of a fundamental importance for aggregation and toxicity of amyloid peptides. In this work, Aβ25-35, a fragment of amyloid β(1-42) (Aβ42), was selected to investigate the correlation between secondary structures and toxicity of amyloid fibrils. Furthermore, each aggregation assemblies show different cell membrane disruption and cytotoxicity. The structural analysis of amyloid aggregates originated from different secondary structure motifs is helpful to understand the mechanism of peptides/cell interactions in the pathogenesis of amyloid diseases.
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