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ASSOCIATE PROFESSOR ERI CHATANI |
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Kobe University chatani@crystal.kobe-u.ac.jp |
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SEMINAR | BIOGRAPHY | ||||
Monday 16th November | Session Six | ||||
Exploring the early stages of protein association in the formation of amyloid fibrils Abstract In this talk, I will present our recent progress on the investigation of early association events of protein molecules during the nucleation process. By using insulin and its derived peptide fragment, we have found that early aggregated species transiently accumulated preceding the formation of amyloid fibrils [3]. From a time-resolved small angle X-ray scattering measurement, we have revealed a rold-like structural property of the early aggregates (MS submitted). After the formation of the early aggregates, they appeared to further coalesce to form larger assemblies, and then be followed by subsequent transconformation towards mature amyloid fibrils. On the basis of these observations, a possible mechanism describing how the amyloidogenic nuclei generate will be discussed. References: |
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2011-present: Associate Professor, Graduate School of Science, Kobe University Research Fields and Interests: Chatani, E., Tsuchisaka, Y., Masuda, Y. and Tsenkova, R. (2014) Water molecular system dynamics associated with amyloidogenic nucleation as revealed by real time near infrared spectroscopy and aquaphotomics. PLOS One 9, e101997. [PMID: 25013915] Chatani, E., Imamura, H., Yamamoto, N. and Kato, M. (2014) Stepwise organization of the β-structure identifies key regions essential for the propagation and cytotoxicity of insulin amyloid fibrils. J. Biol. Chem. 289, 10399-10410. [PMID: 24569992] Chatani, E., Yagi, H., Naiki, H. and Goto, Y. (2012) Polymorphism of β2-microglobulin amyloid fibrils manifested by ultrasonication-enhanced fibril formation in trifluoroethanol. J. Biol. Chem. 287, 22827-22837. [PMID: 22566695] Konuma, T.†, Chatani, E.†, Yagi, M., Sakurai, K., Ikegami, T., Naiki, H. and Goto, Y. (†equally contributed) (2011) Kinetic intermediates of β2-microglobulin fibril elongation probed by pulse-labeling H/D exchange combined with NMR analysis, J. Mol. Biol. 405, 851-862. [PMID: 21108949] Chatani, E., Lee, Y.-H., Yagi, H., Yoshimura, Y., Naiki, H. and Goto, Y. (2009) Ultrasonication-dependent production and breakdown lead to minimum-sized amyloid fibrils. Proc. Natl. Acad. Sci. USA 106, 11119-11124. [PMID: 19564620]
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