l-Arginine reduces thioflavin T fluorescence but not fibrillation of bovine serum albumin
| Autor: | Kuan-Nan Liu, Chih-Yuan Chen, Hsiang-Yun Wang, Steven S.-S. Wang |
|---|---|
| Rok vydání: | 2010 |
| Předmět: |
Amyloid
Protein Conformation Clinical Biochemistry Size-exclusion chromatography Serum albumin macromolecular substances Arginine Fibril Biochemistry Fluorescence chemistry.chemical_compound Microscopy Electron Transmission mental disorders medicine Animals Benzothiazoles Bovine serum albumin Fibrillation Binding Sites Chromatography biology Chemistry Organic Chemistry Serum Albumin Bovine Thiazoles biology.protein Cattle Thioflavin medicine.symptom Protein Binding |
| Zdroj: | Amino Acids. 39:821-829 |
| ISSN: | 1438-2199 0939-4451 |
| DOI: | 10.1007/s00726-010-0536-0 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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