ArticleInternational journal of molecular sciences2023
Monitoring the Conformational Changes of the Aβ(25-35) Peptide in SDS Micelles: A Matter of Time.
Article in International journal of molecular sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed, 8 citations in OpenAlex.
- Gold Nanoparticles Coated With the Antimicrobial Peptide Os-C(W5): Anticandidal and Biological Activity.Journal of peptide science : an official publication of the European Peptide Society · 2026Article
- Conformational determinants of glucagon stability and aggregation kinetics in aqueous and commercial formulations.Protein science : a publication of the Protein Society · 2026Article
- Structural Dynamics of GLP-1 Analogues: Folding Energetics, Lipidation-Driven Assembly, and Aggregation Mechanisms.Molecules (Basel, Switzerland) · 2026Review
- Cell Surface Markers of Mesenchymal Stem Cells: Current Knowledge and Advances in Characterization Technologies.Life (Basel, Switzerland) · 2025Review
- Discovery of a Novel Antimicrobial Peptide fromAntibiotics (Basel, Switzerland) · 2025Article
- A Structural Effect of the Antioxidant Curcuminoids on the Aβ(1-42) Amyloid Peptide.Antioxidants (Basel, Switzerland) · 2025Article
- Neuroprotective Potential of Indole-Based Compounds: A Biochemical Study on Antioxidant Properties and Amyloid Disaggregation in Neuroblastoma Cells.Antioxidants (Basel, Switzerland) · 2024Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Alzheimer's disease is a neurodegenerative disease characterized by the formation of amyloid plaques constituted prevalently by amyloid peptides. Due to the well-known challenges related to the study in solution of these peptides, several membrane-mimicking systems such as micelle constituted by detergent-i.e., DPC and SDS-have been deeply investigated. Additionally, the strategy of studying short fragments instead of the full-length peptide turned out to be advantageous in exploring the structural properties of the different moieties in Aβ in order to reproduce its pathologic effects. Several studies reveal that among Aβ fragments, Aβ(25-35) is the shortest fragment able to reproduce the aggregation process. To enrich the structural data currently available, in the present work we decided to evaluate the conformational changes adopted by Aβ(25-35) in SDS combining CD and NMR spectroscopies at different times. From the solved structures, it emerges that Aβ(25-35) passes from an unordered conformation at the time of the constitution of the system to a more ordered and energetically favorable secondary structure at day 7, which is kept for 2 weeks. These preliminary data suggest that a relatively long time affects the kinetic in the aggregation process of Aβ(25-35) in a micellar system, favoring the stabilization and the formation of a soluble helix conformation.
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