Amyloidogenic protein-membrane interactions: mechanistic insight from model systems.
- Butterfield SM Laboratory of Molecular Neurobiology and Neuroproteomics, Swiss Federal Institute of Technology Lausanne (EPFL), SV-BMI-LMNN AI2351, 1015 Lausanne, Switzerland.
- Lashuel HA
- 2010-07-13
Published in:
- Angewandte Chemie (International ed. in English). - 2010
Amyloid
Amyloid beta-Peptides
Cell Membrane
Islet Amyloid Polypeptide
Lipids
Metals
Models, Biological
Protein Folding
Surface Properties
Synucleins
English
The toxicity of amyloid-forming proteins is correlated with their interactions with cell membranes. Binding events between amyloidogenic proteins and membranes result in mutually disruptive structural perturbations, which are associated with toxicity. Membrane surfaces promote the conversion of amyloid-forming proteins into toxic aggregates, and amyloidogenic proteins, in turn, compromise the structural integrity of the cell membrane. Recent studies with artificial model membranes have highlighted the striking resemblance of the mechanisms of membrane permeabilization of amyloid-forming proteins to those of pore-forming toxins and antimicrobial peptides.
- Language
-
- English
- Open access status
- green
- Identifiers
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- DOI 10.1002/anie.200906670
- PMID 20623810
- Persistent URL
- https://susi.usi.ch/global/documents/105026
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