Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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Seed-dependent Accelerated Fibrillation of ${\alpha}$-Synuclein Induced by Periodic Ultrasonication Treatment

  • Kim, Hyun-Jin (School of Chemical and Biological Engineering, College of Engineering, Seoul National University) ;
  • Chatani, Eri (Institute for Protein Research, Osaka University and CREST, Japan Science and Technology Agency) ;
  • Goto, Yuji (Institute for Protein Research, Osaka University and CREST, Japan Science and Technology Agency) ;
  • Paik, Seung-R. (School of Chemical and Biological Engineering, College of Engineering, Seoul National University)
  • Published : 2007.12.31
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Abstract

[ ${\alpha}$ ]-Synuclein is the major component of Lewy bodies and responsible for the amyloid deposits observed in Parkinson's disease. Ordered filamentous aggregate formation of the natively unfolded ${\alpha}$-synuclein was investigated in vitro with the periodic ultrasonication. The ultrasonication induced the fibrillation of ${\alpha}$-synuclein, as the random structure gradually converted into a ${\beta}$-sheet structure. The resulting fibrils obtained at the stationary phase appeared heterogeneous in their size distribution, with the average length and height of $0.28\;{\mu}m{\pm}0.21\;{\mu}m$ and $5.6\;nm{\pm}1.9\;nm$, respectively. After additional extensive ultrasonication in the absence of monomeric ${\alpha}$-synuclein, the equilibrium between the fibril formation and its breakdown shifted to the disintegration of the preexisting fibrils. The resulting fragments served as nucleation centers for the subsequent seed-dependent accelerated fibrillation under a quiescent incubation condition. This self-seeding amplification process depended on the seed formation and subsequent alterations in their properties by the ultrasonication to a state that accretes the monomeric soluble protein more effectively than their reassociation of the seeds back to the original fibrils. Since many neurodegenerative disorders have been considered to be propagated via the seed-dependent amyloidosis, this study would provide a novel aspect of the significance of the seed structure and its properties leading to the acce]erated amyloid formation.

Keywords

References

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