Parkinson’s disease is a very common neurodegenerative disease and characterized by a progressive loss of the dopaminergic neurons in substantia nigra. The degenerating dopaminergic neurons develop a hallmark deposition of Lewy bodies comprising abundant abnormal aggregates (i.e., fibrils) of α-synuclein (α-syn), which is a protein contains 140 amino acid residues. The primary structure of α-syn constitutes three domains: N-terminal residues 1–60; the nonamyloid component (NAC) which spans residues 61–95 and is responsible for the aggregation; and residues 96–140 which comprise the negatively charged C-terminus. Despite the abundance (~ 1 % among the total proteins) in the brain, α-syn accumulates in the presynaptic terminals where exists high concentration of amphiphilic structure (e.g., lipsomes and cell membrane). Previously, α-syn has been spread at the air-water interface which was used to mimic the amphiphilic nature in vivo. Both circular dichoism (CD) and FTIR results showed that α-syn transform from unstructured conformation in aqueous solution to α-helix at the interface. Here, the NAC part of α-syn (i.e., α-syn(61-95)) was synthesized and purified. α-Syn(61-95) were shown to be also able to form a stable Langmuir monolayer at the air-water interface. From CD results, α-syn(61-95) was shown to be unstructured in aqueous solution and changes to α-helix at the air-water interface. In addition, surface FTIR techniques have shown a parallel orientation of the axis of the helix of α-syn(61-95) to the interface. Due to the high stability at the interface, no aggregation of α-syn(61-95) or α-syn has been detected.

Surface chemistry and spectroscopic study of the NAC part α-synuclein

2019 Spring National Meeting

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