Liu K.-N.Wang H.-Y.Chen C.-Y.Wang S.S.-S.2019-05-092019-05-09201009394451https://scholars.lib.ntu.edu.tw/handle/123456789/406744This 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.AggregateAmyloid fibrilArginineBovine serum albumThT fluorescencejournal article10.1007/s00726-010-0536-02-s2.0-77956917818https://www.scopus.com/inward/record.uri?eid=2-s2.0-77956917818&doi=10.1007%2fs00726-010-0536-0&partnerID=40&md5=6b5ae7a9af66a90f0bf7ad72c3fb044d