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

Autor:	Ling Bo Qu, Li Min Xiong, Sheng Mei Song, Mao Tian Xu, Yong Xiang Wang
Rok vydání:	2012
Předmět:	Depolymerization Stereochemistry Atomic force microscopy macromolecular substances General Chemistry Fibril Fluorescence Fluorescence spectroscopy Baicalein chemistry.chemical_compound Fluorescence intensity chemistry Biophysics Thioflavin
Zdroj:	Chinese Chemical Letters. 23:595-598
ISSN:	1001-8417
DOI:	10.1016/j.cclet.2012.03.001
Popis:	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 β solution which indicating the β -sheet structure of A β fibril. The significant decrease in the intensity of fluorescence at 481 nm was observed when the baicalein was added in mixed solution of A β and ThT, suggesting that the depolymerization of A β fibrils happened and there were A β fibrils left to react with ThT to keep the initial fluorescence intensity. And the existing A β fibrils are disaggregated by baicalein in a time- and dose-dependent manner. AFM images of the morphologies of the A β 1–42 fibrils obviously changed smaller and more dispersive when baicalein added indicating also the depolymerization of A β . The results demonstrate a basis for development of a potential herb drug candidate for the treatment of Alzheimer's disease (AD).
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::490bb62a8e675fcc78ba9bb12dc9391f https://doi.org/10.1016/j.cclet.2012.03.001 Zobrazit plný text záznamu Full Text from ScienceDirect