Amyloids of Alpha-Synuclein Affect the Structure and Dynamics of Supported Lipid Bilayers

A.S. Iyer, N.O. Petersen, Mireille Maria Anna Elisabeth Claessens, Vinod Subramaniam

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27 Citations (Scopus)
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Abstract

Interactions of monomeric alpha-synuclein (αS) with lipid membranes have been suggested to play an important role in initiating aggregation of αS. We have systematically analyzed the distribution and self-assembly of monomeric αS on supported lipid bilayers. We observe that at protein/lipid ratios higher than 1:10, αS forms micrometer-sized clusters, leading to observable membrane defects and decrease in lateral diffusion of both lipids and proteins. An αS 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 αS clusters. These results suggest that the process of amyloid formation, rather than binding of αS on membranes, is crucial in compromising membrane integrity
Original languageEnglish
Pages (from-to)2585-2594
Number of pages10
JournalBiophysical journal
Volume106
Issue number12
DOIs
Publication statusPublished - 2014

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