ArticleChemical science2017
Modulation of electrostatic interactions to reveal a reaction network unifying the aggregation behaviour of the Aβ42 peptide and its variants.
Article in Chemical science, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed.
- Amyloid Beta Oligomers as Early Triggers of Neuronal Cytoskeleton Dysfunction in Alzheimer's Disease.Pathophysiology : the official journal of the International Society for Pathophysiology · 2026Review
- Endogenous Aβ and Exogenous Wheat Gluten Nanostructures: Understanding Peptide Self-Assembly in Disease.ACS nano · 2025Review
- Modulation of Alzheimer's Disease Aβ40 Fibril Polymorphism by the Small Heat Shock Protein αB-Crystallin.Journal of the American Chemical Society · 2024Article
- The role of shear forces in primary and secondary nucleation of amyloid fibrils.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Kinetic models reveal the interplay of protein production and aggregation.Chemical science · 2024Article
- Molecular mechanism of α-synuclein aggregation on lipid membranes revealed.Chemical science · 2024Article
- The thermodynamics of neurodegenerative disease.Biophysics reviews · 2024Review
- Self-replication of AProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Secondary Processes Dominate the Quiescent, Spontaneous Aggregation of α-Synuclein at Physiological pH with Sodium Salts.ACS chemical neuroscience · 2023Article
- Aβ40 Aggregation under Changeable Conditions.International journal of molecular sciences · 2023Article
- Molecular Mechanisms of Amyloid-β Self-Assembly Seeded by In Vivo-Derived Fibrils and Inhibitory Effects of the BRICHOS Chaperone.ACS chemical neuroscience · 2023Article
- The Impact of the Cellular Environment and Aging on Modeling Alzheimer's Disease in 3D Cell Culture Models.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Review
- Simple, Reliable Protocol for High-Yield Solubilization of Seedless Amyloid-β Monomer.ACS chemical neuroscience · 2023Article
- Electrostatic interactions mediate the nucleation and growth of a bacterial functional amyloid.Frontiers in molecular biosciences · 2023Article
- Uncovering the universality of self-replication in protein aggregation and its link to disease.Science advances · 2022Article
- Amyloid-β peptide 37, 38 and 40 individually and cooperatively inhibit amyloid-β 42 aggregation.Chemical science · 2022Article
- Influence of denaturants on amyloid β42 aggregation kinetics.Frontiers in neuroscience · 2022Article
- Mechanistic Models of Protein Aggregation Across Length-Scales and Time-Scales: From the Test Tube to Neurodegenerative Disease.Frontiers in neuroscience · 2022Review
- Dynamic interactions and CaNature communications · 2021Article
- In vivo rate-determining steps of tau seed accumulation in Alzheimer's disease.Science advances · 2021Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
The aggregation of the amyloid β peptide (Aβ42), which is linked to Alzheimer's disease, can be altered significantly by modulations of the peptide's intermolecular electrostatic interactions. Variations in sequence and solution conditions have been found to lead to highly variable aggregation behaviour. Here we modulate systematically the electrostatic interactions governing the aggregation kinetics by varying the ionic strength of the solution. We find that changes in the solution ionic strength induce a switch in the reaction pathway, altering the dominant mechanisms of aggregate multiplication. This strategy thereby allows us to continuously sample a large space of different reaction mechanisms and develop a minimal reaction network that unifies the experimental kinetics under a wide range of different conditions. More generally, this universal reaction network connects previously separate systems, such as charge mutants of the Aβ42 peptide, on a continuous mechanistic landscape, providing a unified picture of the aggregation mechanism of Aβ42.
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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.