Ion Mobility Mass Spectrometry Studies of Alpha Synuclein Fibril ...

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Ion Mobility Mass Spectrometry Studies of the Inhibition of Alpha Synuclein. Amyloid Fibril Formation by (-)-Epigallocatechin-3-Gallate (EGCG). Yanqin Liu, Lam ...
10.1071/CH10334_AC © CSIRO 2011 Australian Journal of Chemistry, 2011, 64(1), 36–40

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Ion Mobility Mass Spectrometry Studies of the Inhibition of Alpha Synuclein Amyloid Fibril Formation by (-)-Epigallocatechin-3-Gallate (EGCG) Yanqin Liu, Lam H. Ho, John. A. Carver and Tara L. Pukala*

School of Chemistry & Physics, The University of Adelaide, Adelaide, South Australia, 5005

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To whom correspondence should be addressed

Email: [email protected]

Phone: +61 8 8303 5497

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Fax: +61 8 8303 4358

Figure S1: Kinetics of A53T α-synuclein fibril formation monitored by the enhancement of thioflavin T fluorescence intensity. Measurements were performed at 37 °C and pH 7.4, with a protein concentration of 20 μM, in the absence (grey) or presence (black) of EGCG at a concentration of 40 μM. ThT fluorescence was excited at 450 nm, and the emission wavelength was 482 nm.

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