CUED Publications database

Chemical properties of lipids strongly affect the kinetics of the membrane-induced aggregation of α-synuclein.

Galvagnion, C and Brown, JWP and Ouberai, MM and Flagmeier, P and Vendruscolo, M and Buell, AK and Sparr, E and Dobson, CM Chemical properties of lipids strongly affect the kinetics of the membrane-induced aggregation of α-synuclein. Proc Natl Acad Sci U S A, 113. pp. 7065-7070. (Unpublished)

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Abstract

Intracellular α-synuclein deposits, known as Lewy bodies, have been linked to a range of neurodegenerative disorders, including Parkinson's disease. α-Synuclein binds to synthetic and biological lipids, and this interaction has been shown to play a crucial role for both α-synuclein's native function, including synaptic plasticity, and the initiation of its aggregation. Here, we describe the interplay between the lipid properties and the lipid binding and aggregation propensity of α-synuclein. In particular, we have observed that the binding of α-synuclein to model membranes is much stronger when the latter is in the fluid rather than the gel phase, and that this binding induces a segregation of the lipids into protein-poor and protein-rich populations. In addition, α-synuclein was found to aggregate at detectable rates only when interacting with membranes composed of the most soluble lipids investigated here. Overall, our results show that the chemical properties of lipids determine whether or not the lipids can trigger the aggregation of α-synuclein, thus affecting the balance between functional and aberrant behavior of the protein.

Item Type: Article
Uncontrolled Keywords: Parkinson’s disease lipid-induced aggregation phase diagram α-synuclein Cell Membrane Humans Kinetics Lipid Bilayers Parkinson Disease Protein Aggregation, Pathological alpha-Synuclein
Subjects: UNSPECIFIED
Divisions: Div B > Solid State Electronics and Nanoscale Science
Depositing User: Cron Job
Date Deposited: 17 Jul 2017 18:57
Last Modified: 14 Dec 2017 02:19
DOI: