ArticleThe Journal of biological chemistry2013
Formation of dynamic soluble surfactant-induced amyloid β peptide aggregation intermediates.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 52 citations in OpenAlex.
- Article
- Morphological and Molecular Profiling of Amyloid-β Species in Alzheimer's Pathogenesis.Molecular neurobiology · 2025Review
- Guide to the structural characterization of protein aggregates and amyloid fibrils by CD spectroscopy.Protein science : a publication of the Protein Society · 2025Article
- Current understanding of metal-dependent amyloid-β aggregation and toxicity.RSC chemical biology · 2023Review
- Amyloid Disassembly: What Can We Learn from Chaperones?Biomedicines · 2022Review
- The intriguing dose-dependent effect of selected amphiphilic compounds on insulin amyloid aggregation: Focus on a cholesterol-based detergent, Chobimalt.Frontiers in molecular biosciences · 2022Article
- Cationic gemini surfactant stimulates amyloid fibril formation in bovine liver catalase at physiological pH. A biophysical study.RSC advances · 2020Article
- Diverse Structural Conversion and Aggregation Pathways of Alzheimer's Amyloid-β (1-40).ACS nano · 2019Article
- Refolding of SDS-Unfolded Proteins by Nonionic Surfactants.Biophysical journal · 2017Article
- Interaction of the amyloid β peptide with sodium dodecyl sulfate as a membrane-mimicking detergent.Journal of biological physics · 2016Article
- Article
- Self protein-protein interactions are involved in TPPP/p25 mediated microtubule bundling.Scientific reports · 2015Article
- Zinc as chaperone-mimicking agent for retardation of amyloid β peptide fibril formation.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Lysophospholipid-containing membranes modulate the fibril formation of the repeat domain of a human functional amyloid, pmel17.Journal of molecular biology · 2014Article
- Distinct synthetic Aβ prion strains producing different amyloid deposits in bigenic mice.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- The hairpin conformation of the amyloid β peptide is an important structural motif along the aggregation pathway.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2014Review
- The C-terminal threonine of Aβ43 nucleates toxic aggregation via structural and dynamical changes in monomers and protofibrils.Biochemistry · 2014Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Intermediate amyloidogenic states along the amyloid β peptide (Aβ) aggregation pathway have been shown to be linked to neurotoxicity. To shed more light on the different structures that may arise during Aβ aggregation, we here investigate surfactant-induced Aβ aggregation. This process leads to co-aggregates featuring a β-structure motif that is characteristic for mature amyloid-like structures. Surfactants induce secondary structure in Aβ in a concentration-dependent manner, from predominantly random coil at low surfactant concentration, via β-structure to the fully formed α-helical state at high surfactant concentration. The β-rich state is the most aggregation-prone as monitored by thioflavin T fluorescence. Small angle x-ray scattering reveals initial globular structures of surfactant-Aβ co-aggregated oligomers and formation of elongated fibrils during a slow aggregation process. Alongside this slow (minutes to hours time scale) fibrillation process, much faster dynamic exchange (k(ex) ∼1100 s(-1)) takes place between free and co-aggregate-bound peptide. The two hydrophobic segments of the peptide are directly involved in the chemical exchange and interact with the hydrophobic part of the co-aggregates. Our findings suggest a model for surfactant-induced aggregation where free peptide and surfactant initially co-aggregate to dynamic globular oligomers and eventually form elongated fibrils. When interacting with β-structure promoting substances, such as surfactants, Aβ is kinetically driven toward an aggregation-prone state.
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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.