单宁酸的抗淀粉样蛋白生成活性及其体外破坏阿尔茨海默β -淀粉样蛋白原纤维的活性。

Kenjiro Ono, Kazuhiro Hasegawa, Hironobu Naiki, Masahito Yamada
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引用次数: 242

摘要

抑制淀粉样蛋白-肽(Abeta)的积累和由β -淀粉样蛋白原纤维(fAbeta)形成的β -淀粉样蛋白原纤维(fAbeta),以及在中枢神经系统中预先形成的fAbeta的不稳定,将是治疗阿尔茨海默病(AD)的有吸引力的治疗靶点。我们之前报道过去甲二氢愈创木酸(NDGA)和葡萄酒相关的多酚在体外剂量依赖性地抑制Abeta(1-40)和Abeta(1-42)形成fAbeta,以及破坏预形成的fAbeta(1-40)和fAbeta(1-42)的稳定性。利用荧光光谱分析与硫黄素T和电镜研究,我们研究了聚合多酚,单宁酸(TA)对fAbeta(1-40)和fAbeta(1-42)在pH 7.5, 37℃下的形成,延伸和不稳定的影响。接下来,我们比较了TA与杨梅素、利福平、四环素和NDGA的抗淀粉样蛋白生成活性。TA剂量依赖性地抑制Abeta(1-40)和Abeta(1-42)的fAbeta形成及其延伸。此外,它还能剂量依赖性地破坏预制的fabeta。TA对fabeta的形成、延伸和失稳的有效浓度(EC50)在0 ~ 0.1 μ m之间。尽管TA在体外抑制fAbeta形成以及破坏预先形成的fAbeta的机制尚不清楚,但它可能是开发AD治疗方法的关键分子。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Anti-amyloidogenic activity of tannic acid and its activity to destabilize Alzheimer's beta-amyloid fibrils in vitro.

Inhibition of the accumulation of amyloid beta-peptide (Abeta) and the formation of beta-amyloid fibrils (fAbeta) from Abeta, as well as the destabilization of preformed fAbeta in the CNS would be attractive therapeutic targets for the treatment of Alzheimer's disease (AD). We previously reported that nordihydroguaiaretic acid (NDGA) and wine-related polyphenols inhibit fAbeta formation from Abeta(1-40) and Abeta(1-42) as well as destabilizing preformed fAbeta(1-40) and fAbeta(1-42) dose-dependently in vitro. Using fluorescence spectroscopic analysis with thioflavin T and electron microscopic studies, we examined the effects of polymeric polyphenol, tannic acid (TA) on the formation, extension, and destabilization of fAbeta(1-40) and fAbeta(1-42) at pH 7.5 at 37 degrees C in vitro. We next compared the anti-amyloidogenic activities of TA with myricetin, rifampicin, tetracycline, and NDGA. TA dose-dependently inhibited fAbeta formation from Abeta(1-40) and Abeta(1-42), as well as their extension. Moreover, it dose-dependently destabilized preformed fAbetas. The effective concentrations (EC50) of TA for the formation, extension and destabilization of fAbetas were in the order of 0-0.1 microM. Although the mechanism by which TA inhibits fAbeta formation from Abeta as well as destabilizes preformed fAbeta in vitro is still unclear, it could be a key molecule for the development of therapeutics for AD.

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