Studies on the Interaction Between Vanillin and β-Amyloid Protein via Fluorescence Spectroscopy and Atomic Force Microscopy

doi:10.1007/s40242-016-5347-8

Abstract

Abstract:

β-Amyloid(Aβ) plaques and intracellular neurofibrillary lesions in the brain are markers of Alzheimer's disease(AD). The ability to safely decrease Aβ concentrations is potentially important as a preventive strategy for AD. The interactions between vanillin and Aβ polypeptide were investigated via fluorescence spectroscopy and atomic force microscopy(AFM). The results of fluorescence and synchronous spectroscopies illustrate that the intrinsic fluorescence of tyrosine(Tyr) residues in Aβ_1-42 aggregates can be quenched strongly upon the formation of vanillin-Aβ_1-42 complex. Thioflavine T(ThT)-induced fluorescence changes indicated that Aβ_1-42 aggregates could be disaggregated by vanillin, and the AFM images of Aβ_1-42 enunciated the depolymerization of Aβ_1-42 aggregates by vanillin in a dose-dependent manner. Vanillin may be a potential pharmacological agent for the treatment of AD.

Key words: β-Amyloid fibril, Vanillin, Interaction, Fluorescence spectroscopy, Atomic force microscopy

SONG Shengmei, MA Xuewen, ZHOU Yehong, XU Maotian, SHUANG Shaomin, DONG Chuan. Studies on the Interaction Between Vanillin and β-Amyloid Protein via Fluorescence Spectroscopy and Atomic Force Microscopy[J]. Chemical Research in Chinese Universities, 2016, 32(2): 172-177.

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