Effect of the Interaction of the Amyloid beta (1-42) Peptide with Short Single-Stranded Synthetic Nucleotide Sequences: Morphological Characterization of the Inhibition of Fibrils Formation and Fibrils Disassembly
| Autor: | Jancy Nixon Abraham, Enora Prado, Dawid Kedracki, Corinne Nardin, Plinio Maroni, Charlotte Gourmel |
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| Přispěvatelé: | Department of Inorganic, Analytical and Applied Chemistry, Laboratory of Colloid and Surface Chemistry (LCSC), Université de Genève (UNIGE)-Université de Genève (UNIGE), Department of Inorganic and Analytical Chemistry - University of Geneva, Institut des sciences analytiques et de physico-chimie pour l'environnement et les materiaux (IPREM), Université de Pau et des Pays de l'Adour (UPPA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS) |
| Jazyk: | angličtina |
| Rok vydání: | 2014 |
| Předmět: |
Polymers and Plastics
Amyloid beta Oligonucleotides Bioengineering Context (language use) Peptide Fibril Protein Aggregation Pathological Biomaterials Alzheimer Disease Spectroscopy Fourier Transform Infrared Materials Chemistry Extracellular Humans [CHIM]Chemical Sciences Synthetic nucleotide Senile plaques chemistry.chemical_classification Amyloid beta-Peptides biology Chemistry Polyelectrolyte Peptide Fragments Biochemistry ddc:540 biology.protein Biophysics |
| Zdroj: | Biomacromolecules Biomacromolecules, American Chemical Society, 2014, 15 (9), pp.3253-3258. ⟨10.1021/bm501004q⟩ BIOMACROMOLECULES Biomacromolecules, Vol. 15, No 9 (2014) pp. 3253-3258 |
| ISSN: | 1525-7797 1526-4602 |
| Popis: | International audience; The formation of extracellular neuritic plaques in the brain of individuals who suffered from Alzheimer’s disease (AD) is a major pathological hallmark. These plaques consist of filamentous aggregates of the amyloid beta (1–42) (Aβ42) proteins. Prevention or reduction of the formation of these fibrils is foreseen as a potential therapeutic approach. In this context, we investigated the interactions between the Aβ42 protein and polyions, in particular short single stranded synthetic nucleotide sequences. The experimental outcomes reported herein provide evidence of the inhibition of amyloid fibril genesis as well as disassembly of existing fibers through electrostatic interaction between the Aβ42 protein and the polyions. Since the polyions and the Aβ42 protein are oppositely charged, the formation of (micellar) inter polyelectrolyte complexes (IPECs) is likely to occur. Since the abnormal deposition of amyloid fibers is an archetype of AD, the outcomes of these investigations, supported by atomic force microscopy imaging in the dry and liquid states, as well as circular dichroism and Fourier transform infrared spectroscopy, are of high interest for the development of future strategies to cure a disease that concerns an ever aging population. |
| Databáze: | OpenAIRE |
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