Utilizing magnetic resonance techniques to study membrane interactions of amyloid peptides
| Autor: | David W. Keizer, Marc-Antoine Sani, Sunnia Rajput, Frances Separovic |
|---|---|
| Rok vydání: | 2021 |
| Předmět: |
Amyloid
Magnetic Resonance Spectroscopy Amyloid beta Cell Biophysics Plaque Amyloid 010402 general chemistry 01 natural sciences Biochemistry Amyloid beta-Protein Precursor 03 medical and health sciences chemistry.chemical_compound NMR spectroscopy Alzheimer Disease Structural Biology Extracellular medicine Humans Cytotoxic T cell Review Articles phospholipids 030304 developmental biology Neurons 0303 health sciences Amyloid beta-Peptides Molecular Interactions biology Cell Membrane Brain Nuclear magnetic resonance spectroscopy Beta-peptide 0104 chemical sciences amyloid beta Alzheimers disease medicine.anatomical_structure Membrane chemistry membranes Synapses biology.protein Protein Binding |
| Zdroj: | Biochemical Society Transactions |
| ISSN: | 1470-8752 0300-5127 |
| DOI: | 10.1042/bst20201244 |
| Popis: | Alzheimer's disease (AD) is a common neurodegenerative condition that involves the extracellular accumulation of amyloid plaques predominantly consisting of Aβ peptide aggregates. The amyloid plaques and soluble oligomeric species of Aβ are believed to be the major cause of synaptic dysfunction in AD brain and their cytotoxic mechanisms have been proposed to involve interactions with cell membranes. In this review, we discuss our solid-state nuclear magnetic resonance (ssNMR) studies of Aβ interactions with model membranes. |
| Databáze: | OpenAIRE |
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