https://scholars.lib.ntu.edu.tw/handle/123456789/406744
Title: | L-Arginine reduces thioflavin T fluorescence but not fibrillation of bovine serum album | Authors: | Liu K.-N. Wang H.-Y. Chen C.-Y. Wang S.S.-S. |
Keywords: | Aggregate;Amyloid fibril;Arginine;Bovine serum album;ThT fluorescence | Issue Date: | 2010 | Journal Volume: | 39 | Journal Issue: | 3 | Start page/Pages: | 821-829 | Source: | Amino Acids | Abstract: | This work examines the effects of L-arginine (L-Arg) on the aggregation and amyloid fibrillation of bovine serum albumin (BSA). We demonstrate that L-Arg dose-dependently reduces thioflavin T (ThT) fluorescence of BSA within the L-Arg concentration range used (0-1.4 M). However, as revealed by electron microscopy, size exclusion chromatography, and dynamic light scattering results, L-Arg does not prevent amyloid-like fibril formation by BSA. We conclude that L-Arg competes against ThT for binding sites on BSA amyloid-like fibrils, leading to biased results in ThT fluorescence measurements. Moreover, the use of ThT fluorescence assay to screen for potential inhibitors against amyloid fibrillation can give misleading results. ? Springer-Verlag 2010. |
URI: | https://scholars.lib.ntu.edu.tw/handle/123456789/406744 | ISSN: | 09394451 | DOI: | 10.1007/s00726-010-0536-0 |
Appears in Collections: | 化學工程學系 |
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