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首页> 外文期刊>Amino acids >L-Arginine reduces thioflavin T fluorescence but not fibrillation of bovine serum albumin
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L-Arginine reduces thioflavin T fluorescence but not fibrillation of bovine serum albumin

机译:L-精氨酸可降低硫代黄素T荧光,但不会降低牛血清白蛋白的原纤化

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摘要

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.
机译:这项工作检查了L-精氨酸(L-Arg)对牛血清白蛋白(BSA)聚集和淀粉样原纤维化的影响。我们证明L-Arg在所用L-Arg浓度范围内(0-1.4 M)剂量依赖性地降低BSA的硫黄素T(ThT)荧光。但是,如通过电子显微镜,尺寸排阻色谱法和动态光散射结果所揭示的,L-Arg不能阻止BSA形成淀粉样样原纤维。我们得出的结论是,L-Arg与ThT竞争BSA淀粉样蛋白样原纤维上的结合位点,导致ThT荧光测量结果出现偏差。此外,使用ThT荧光测定法筛选潜在的抗淀粉样蛋白原纤化抑制剂可能会产生误导性的结果。

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