期刊
LANGMUIR
卷 38, 期 33, 页码 10216-10224出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.langmuir.2c01368
关键词
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资金
- Center for High Resolution Neutron Scattering
- National Institute of Standards and Technology
- National Science Foundation [DMR-2010792]
- Swedish Foundation for Strategic Research through the national Graduate School SwedNessESS [GSn15- 0008]
- Swedish Research Council VR [ES 2014-03971, SL 2015-00143]
- Knut and Alice Wallenberg Foundation [UO 2016.0074]
The study reports the interaction between alpha-Synuclein and model membranes, showing that circular discs undergo shape transition after the adsorption of aSyn. When aSyn self-assembles into fibrils, aSyn molecules desorb from the bilayer discs, allowing them to recover to their original shape.
alpha-Synuclein (aSyn) is a 140 residue long protein present in presynaptic termini of nerve cells. The protein is associated with Parkinson's disease, in which case it has been found to self-assemble into long amyloid fibrils forming intra-cellular inclusions that are also rich in lipids. Furthermore, its synaptic function is proposed to involve interaction with lipid membranes, and hence, it is of interest to understand aSyn-lipid membrane interactions in detail. In this paper we report on the interaction of aSyn with model membranes in the form of lipid bilayer discs. Using a combination of cryogenic transmission electron microscopy and small-angle neutron scattering, we show that circular discs undergo a significant shape transition after the adsorption of aSyn. When aSyn self-assembles into fibrils, aSyn molecules desorb from the bilayer discs, allowing them to recover to their original shape. Interestingly, the desorption process has an all-or-none character, resulting in a binary coexistence of circular bilayer discs with no adsorbed aSyn and deformed bilayer discs having a maximum amount of adsorbed protein. The observed coexistence is consistent with the recent finding of cooperative aSyn adsorption to anionic lipid bilayers.
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