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The interplay between lipids and dopamine on ?-synuclein oligomerisation and membrane binding.
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Biosci Rep 2013 Sep;
Authors: Chi L L Pham, Roberto Cappai
The deposition of ?-synuclein (?-syn) as amyloid fibrils and the selective loss of dopamine (DA) containing neurons in the substantia nigra are two key features of Parkinson's disease (PD). ?-Syn is a natively unfolded protein and adopts an ?-helical conformation upon binding to lipid membrane. Oligomeric species of ?-syn have been proposed to be the pathogenic species associated with PD because they can bind lipid membranes and disrupt membrane integrity. DA is readily oxidised to generate reactive intermediates and reactive oxygen species (ROS) and in the presence of DA, ?-syn form SDS-resistant soluble oligomers. It is postulated that the formation of the ?-syn:DA oligomers involves the cross-linking of DA-melanin with ?-syn, via covalent linkage, hydrogen and hydrophobic interactions. We investigate the effect of lipids on DA-induced ?-syn oligomerisation and studied the ability of ?-syn:DA oligomers to interact with lipids vesicles. Our results show that the interaction of ?-syn with lipids inhibits the formation of DA-induced ?-syn oligomers. Moreover, the ?-syn:DA oligomer can not interact with lipid vesicles or cause membrane permeability. Thus, the formation of ?-syn:DA oligomers may alter the actions of ?-syn which require membrane association, leading to disruption of its normal cellular function.
PMID: 24066973 [PubMed - as supplied by publisher]