AFM and fluorescence spectrascopy investigation for disaggregation of existing A尾 fibrils by baicalein

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• 作者：Sheng Mei Song^a ; ^b ; Yong Xiang Wang^b ; Li Min Xiong^b ; Ling Bo Qu^a ; ^{qulingbo@zzu.edu.cn} ; Mao Tian Xu^a ; ^b ; ^{xumaotian@163.com}
• 关键词：Amyloid 尾 peptide ; Baicalein ; Fluorescence spectroscopy ; Atomic force microscope
• 刊名：Chinese Chemical Letters
• 出版年：2012
• 期刊代码：3_10018417
• 类别：ch
• 出版时间：May, 2012
• 卷：23
• 期：5
• 页码：595-598
• 文件大小：946 K

摘要

The wavelength for the peak of fluorescence emission of thioflavin T (ThT) was changed from 445 nm to 481 nm when ThT was added in A尾 solution which indicating the 尾-sheet structure of A尾 fibril. The significant decrease in the intensity of fluorescence at 481 nm was observed when the baicalein was added in mixed solution of A尾 and ThT, suggesting that the depolymerization of A尾 fibrils happened and there were A尾 fibrils left to react with ThT to keep the initial fluorescence intensity. And the existing A尾 fibrils are disaggregated by baicalein in a time- and dose-dependent manner. AFM images of the morphologies of the A尾_1-42 fibrils obviously changed smaller and more dispersive when baicalein added indicating also the depolymerization of A尾. The results demonstrate a basis for development of a potential herb drug candidate for the treatment of Alzheimer's disease (AD).