|Title:||L-Arginine reduces thioflavin T fluorescence but not fibrillation of bovine serum album||Authors:||Liu K.-N.
|Keywords:||Aggregate;Amyloid fibril;Arginine;Bovine serum album;ThT fluorescence||Issue Date:||2010||Source:||Amino Acids||Journal Volume:||39||Journal Issue:||3||Start page/Pages:||821-829||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.
|Appears in Collections:||化學工程學系|
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.