Studies on the interaction between vanillin and β -Amyloid protein via fluorescence spectroscopy and atomic force microscopy

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.