| Autor: |
Atassi, M. Zouhair, Berliner, Lawrence J., Chang, Rowen Jui-Yoa, Jörnvall, Hans, Kenyon, Geroge L., Wittman-Liebold, Brigitie, Uversky, Vladimir N., Fink, Anthony L., Ban, Tadato, Goto, Yuji |
| Zdroj: |
Protein Misfolding, Aggregation & Conformational Diseases (978-0-387-25918-5); 2006, p335-343, 9p |
| Abstrakt: |
Amyloid fibril formation is a phenomenon common to many proteins and peptides associated with numerous conformational diseases. To clarify the mechanism of fibril formation and to create inhibitors, real-time monitoring of fibril growth is essential. This chapter describes a method to visualize amyloid fibril growth in real time at the single fibril level. This approach uses total internal reflection fluorescence microscopy (TIRFM) combined with the binding of thioflavin T, an amyloidspecifi c fluorescence dye. The method enables an exact analysis of the rate of growth of individual fibrils. One of the advantages of TIRFM is that only amyloid fibrils lying in parallel with the slide glass surface were observed, so that one can obtain the exact length of fibrils. This method is of particular importance for the analysis of rapid fibrillation kinetics, providing unique information crucial for the elucidation of the molecular mechanisms of amyloid fibril formation. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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