期刊
AMINO ACIDS
卷 39, 期 3, 页码 821-829出版社
SPRINGER WIEN
DOI: 10.1007/s00726-010-0536-0
关键词
Amyloid fibril; Aggregate; Arginine; ThT fluorescence; Bovine serum albumin
资金
- National Science Council, Taiwan
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.
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