The protein α-synuclein has been heavily implicated in the development of multiple neurodegenerative diseases, notably Parkinson’s disease. While its natural function is still unknown, α-synuclein is suspected to be involved with the regulation of neurotransmitter vesicles, due to its well-known behavior for forming α-helical secondary structures upon binding to acidic phospholipid vesicles, as well as its high affinity to these anionic vesicles. However, due to the malleable nature of vesicles and liposomes, it is difficult to ensure the retention of their size, shape, and structure after protein binding. In fact, α-synuclein has been shown previously to possess the ability to deform lipid vesicles into tubular structures. To circumvent this, we functionalized gold nanoparticles with diameters ranging from 12 - 90 nm with a hybrid lipid bilayer in order to “fix” the radius of curvature of the liposome. A gold core in the center of these hybrid liposomes adds useful optical and photothermal properties to these lipid vesicles. The results of this study suggest that wildtype α-synuclein shows high tendencies for forming α-helical structures when bound to lipid nanoparticles with diameters of 12 – 20 nm and 65 – 85 nm; surprisingly, α-synuclein seems to adopt a different protein conformation when bound to lipid nanoparticles with diameters 30 – 45 nm.

Fixed membranes for the study of wildtype α-synuclein’s binding to lipid bilayers

251st National Meeting (2016)

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