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Originally published In Press as doi:10.1074/jbc.C300049200 on March 18, 2003

J. Biol. Chem., Vol. 278, Issue 19, 16462-16465, May 9, 2003
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ACCELERATED PUBLICATION
Direct Observation of Amyloid Fibril Growth Monitored by Thioflavin T Fluorescence*,

Tadato BanDagger §, Daizo HamadaDagger §, Kazuhiro Hasegawa||, Hironobu Naiki||, and Yuji GotoDagger **

From the Dagger  Institute for Protein Research, Osaka University and Core Research for Evolutional Science and Technology (CREST), Japan Science and Technology Cooperation, 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan and the || Department of Pathology, Fukui Medical University and CREST, Japan Science and Technology Corporation, Matsuoka, Fukui 910-1193, Japan

Real-time monitoring of fibril growth is essential to clarify the mechanism of amyloid fibril formation. Thioflavin T (ThT) is a reagent known to become strongly fluorescent upon binding to amyloid fibrils. Here, we show that, by monitoring ThT fluorescence with total internal reflection fluorescence microscopy (TIRFM), amyloid fibrils of beta 2-microgobulin (beta 2-m) can be visualized without requiring covalent fluorescence labeling. One of the advantages of TIRFM would be that we selectively monitor fibrils lying along the slide glass, so that we can obtain the exact length of fibrils. This method was used to follow the kinetics of seed-dependent beta 2-m fibril extension. The extension was unidirectional with various rates, suggesting the heterogeneity of the amyloid structures. Since ThT binding is common to all amyloid fibrils, the present method will have general applicability for the analysis of amyloid fibrils. We confirmed this with the octapeptide corresponding to the C terminus derived from human medin and the Alzheimer's amyloid beta -peptide.

* This work was supported by grants-in-aid for scientific research from the Japanese Ministry of Education, Science, Culture and Sports.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this journal (available at http://www.jbc.org) contains a movie file (b2m.mov): the growth processes of amyloid fibrils monitored by ThT fluorescence with total internal reflection fluorescence microscopy, as shown in Fig. 2, E-H.

§ These authors contributed equally.

Supported by Japan Society for Promotion of Science Research Fellowships for Young Scientists. Present address: Dept. of Developmental Infectious Diseases, Research Inst. and Osaka Medical Center for Maternal and Child Health, 840 Murodo-cho, Izumi, Osaka 594-1011, Japan.

** To whom correspondence should be addressed: Inst. for Protein Research, Osaka University 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan. Tel.: 81-6-6879-8614; Fax: 81-6-6879-8616; E-mail: ygoto@protein.osaka-u.ac.jp.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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