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

β -Amyloid(A β ) plaques and intracellular neurofibrillary lesions in the brain are markers of Alzheimer’s disease(AD). The ability to safely decrease A β concentrations is potentially important as a preventive strategy for AD. The interactions between vanillin and A β 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 A β 1-42 aggregates can be quenched strongly upon the formation of vanillin-A β 1-42 complex. Thioflavine T(ThT)-induced fluorescence changes indicated that A β 1-42 aggregates could be disaggregated by vanillin, and the AFM images of A β 1-42 enunciated the depolymerization of A β 1-42 aggregates by vanillin in a dose-dependent manner. Vanillin may be a potential pharmacological agent for the treatment of AD.