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首页> 外文期刊>Biochemistry >The anti-amyloidogenic effect is exerted against Alzheimer's beta-amyloid fibrils in vitro by preferential and reversible binding of flavonoids to the amyloid fibril structure.
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The anti-amyloidogenic effect is exerted against Alzheimer's beta-amyloid fibrils in vitro by preferential and reversible binding of flavonoids to the amyloid fibril structure.

机译：通过类黄酮与淀粉样蛋白原纤维结构的优先和可逆结合，在体外对阿尔茨海默氏症的β-淀粉样蛋白原纤维具有抗淀粉样作用。

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摘要

How various anti-amyloidogenic compounds inhibit the formation of Alzheimer's beta-amyloid fibrils (fAbeta) from amyloid beta-peptide (Abeta) and destabilize fAbeta remains poorly understood. Using spectrophotometry, spectrofluorometry, atomic force microscopy, sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and surface plasmon resonance (SPR), we investigated the anti-amyloidogenic effects of five flavonoids on fAbeta in vitro. Oxidized flavonoids generally inhibited fAbeta(1-40) formation significantly more potently than fresh compounds. Characterization of the novel fluorescence of myricetin (Myr) emitted at 575 nm with an excitation maximum at 430 nm in the presence of fAbeta(1-40) revealed the specific binding of Myr to fAbeta(1-40). By SPR analysis, distinct association and dissociation reactions of Myr with fAbeta(1-40) were observed, in contrast to the very weak binding to the Abeta monomer. A significant decrease in the rate of fibril extension was observed when >0.5 microM Myr was injected into the SPR experimental system. These findings suggest that flavonoids, especially Myr, exert an anti-amyloidogenic effect in vitro by preferentially and reversibly binding to the amyloid fibril structure of fAbeta, rather than to Abeta monomers.
机译：各种抗淀粉样蛋白化合物如何抑制淀粉状蛋白β肽（Abeta）形成的阿尔茨海默氏病β-淀粉样蛋白原纤维（fAbeta）并破坏fAbeta的稳定性仍知之甚少。使用分光光度法，荧光光谱法，原子力显微镜，十二烷基硫酸钠-聚丙烯酰胺凝胶电泳和表面等离子体共振（SPR），我们研究了5种类黄酮在体外对fAbeta的抗淀粉样蛋白作用。氧化的类黄酮通常比新鲜化合物更有效地抑制fAbeta（1-40）的形成。在存在fAbeta（1-40）的情况下，在575 nm发射的杨梅素（Myr）的新型荧光的表征最大激发波长为430 nm，揭示了Myr与fAbeta（1-40）的特异性结合。通过SPR分析，观察到Myr与fAbeta（1-40）的明显缔合和解离反应，而与Abeta单体的结合非常弱。当将> 0.5 microM Myr注入SPR实验系统时，观察到原纤维延伸速率的显着降低。这些发现表明，类黄酮，特别是Myr，通过优先和可逆地结合到fAbeta的淀粉样蛋白原纤维结构而不是Abeta单体上，发挥抗淀粉样蛋白作用。

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