Journal
BIOPHYSICAL JOURNAL
Volume 106, Issue 12, Pages 2585-2594Publisher
CELL PRESS
DOI: 10.1016/j.bpj.2014.05.001
Keywords
-
Categories
Funding
- A Single Molecule View on Protein Aggregation
- Netherlands Organization for Scientific Research [040-11-389]
Ask authors/readers for more resources
Interactions of monomeric alpha-synuclein (alpha S) with lipid membranes have been suggested to play an important role in initiating aggregation of alpha S. We have systematically analyzed the distribution and self-assembly of monomeric alpha S on supported lipid bilayers. We observe that at protein/lipid ratios higher than 1:10, alpha S forms micrometer-sized clusters, leading to observable membrane defects and decrease in lateral diffusion of both lipids and proteins. An alpha S deletion mutant lacking amino-acid residues 71-82 binds to membranes, but does not observably affect membrane integrity. Although this deletion mutant cannot form amyloid, significant amyloid formation is observed in the wild-type alpha S clusters. These results suggest that the process of amyloid formation, rather than binding of alpha S on membranes, is crucial in compromising membrane integrity.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available