The insoluble fiber formation of the a-synuclein peptide is regarded as a major pathological hallmark of Parkinson's disease. The mechanism of fiber formation is speculated to involve an intermediate oligomers, and the detailed investigation of the oligomers has been challenging. We made an approach to stably conform the oligomeric forms by using the surface potential of a nanoparticle, and observed a reversible self-assembly over 60 nm gold colloid through a repetitive change of pH between pH4 and pH 10. We concluded that an a-synuclein monomer forms an unfolded conformation at pH 4 and re-assembled to a folded conformation at pH 10, repetitively.  The smaller size than 60 nm did not exhibit any signs of this reversible self-assembly, and it implies that there is a threshold surface area at over that value, enough surface potential to support stable oligomers.

Reversible self-assembly of a-synuclein peptide on gold colloidal nanoparticles' surfaces

248th National Meeting (2014)

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