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l-Arginine reduces thioflavin T fluorescence but not fibrillation of bovine serum albumin

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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.

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Acknowledgments

This work was supported by grants from the National Science Council, Taiwan.

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Authors and Affiliations

  1. Department of Chemical Engineering, National Taiwan University, No. 1, Sec. 4, Roosevelt Rd., Taipei, 10617, Taiwan

    Kuan-Nan Liu, Hsiang-Yun Wang, Chih-Yuan Chen & Steven S.-S. Wang

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  1. Kuan-Nan Liu
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  2. Hsiang-Yun Wang
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Correspondence to Steven S.-S. Wang.

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Liu, KN., Wang, HY., Chen, CY. et al. l-Arginine reduces thioflavin T fluorescence but not fibrillation of bovine serum albumin. Amino Acids 39, 821–829 (2010). https://doi.org/10.1007/s00726-010-0536-0

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