【作者】 宋胜梅； 王永祥； 熊利敏； 徐茂田； 屈凌波；

【Author】 ShengmeiSong 1,2,Y Wang 1,L Xiong 1,M Xu 1,2,,L Qu 1,2, 1.Henan Key Laboratory Cultivation Base of Nanobiological Analytical Chemistry,College of Chemistry and Chemical Engineering,Shangqiu Normal University,Shangqiu,476000,China 2.Department of Chemistry,Zhengzhou University,Zhengzhou,450052,China

【机构】 商丘师范学院化学化工学院； 郑州大学化学系；

【摘要】 <正>最近的研究表明,贝加因可通过保护神经而缓解Aβ25-35诱导的健忘症,并可能降低氧化应激从而减少PC12细胞中Aβ蛋白的细胞毒性[1-3]。我们用荧光光谱和紫外-可见光谱法研究了贝加因和Aβ相互作用的原更多还原

【Abstract】 The interaction between baicalein with amyloid-β(Aβ) polypeptide was investigated by fluorescence and UV–Vis absorbance spectroscopy.The absence of the characteristic tyrosinate(Tyr) peak in the absorption spectra of Aβ-baicalein complexes provided evidence that the sole Tyr residue in Aβ is not bound to baicalein,but remains close to it.The intrinsic fluorescence of Tyr residues in Aβ 1-42 aggregates was quenched strongly by excited-state ionization by baicalein.In this complex the hydroxyl group was not ionized,but was prepared to ionize immediately upon excitation.Absorbance,fluorescence and synchronous spectroscopy denominated that the form of Schiff base between the quinone of baicalein and the Lys side chains of Aβ 1-42 is another major reason in the depolymerization of Aβ 1-42 aggregates by baicalein.It is wished that this paper could offer some valuable references for the application of flavonoid derivants in Alzheimer’s disease treatment.更多还原