$\beta$-amyloid amorphous aggregates induced by the small natural molecule ferulic acid

Title$\beta$-amyloid amorphous aggregates induced by the small natural molecule ferulic acid
Publication TypeJournal Article
Year of Publication2013
AuthorsBramanti, E, Fulgentini, L, Bizzarri, R, Lenci, F, Sgarbossa, A
JournalJournal of Physical Chemistry B
ISSN15206106 (ISSN)
KeywordsAggregates, Alzheimer's disease, amyloid beta protein, amyloid beta protein[1-40], Amyloid beta-Peptides, Article, chemistry, Chromatographic analysis, coumaric acid, Coumaric Acids, Electrophoresis, ferulic acid, Ferulic acids, Fibrillogenesis, Fluorescence, fluorescence microscopy, Fourier Transform Infrared, Fourier transform infrared spectroscopy, Fruit and vegetables, Glycoproteins, Infrared spectroscopy, Kinetics, metabolism, Microscopy, Molecular basis, Molecules, Neurodegenerative diseases, Neurodegenerative disorders, peptide fragment, Peptide Fragments, Phenolic compounds, Protein Binding, Spectroscopy, Temperature, Therapeutic use

There is an emerging interest in small natural molecules for their potential therapeutic use in neurodegenerative disorders like Alzheimer's disease (AD). Ferulic acid (FA), an antioxidant phenolic compound present in fruit and vegetables, has been proposed as an inhibitor of beta amyloid (A$\beta$) pathological aggregation. Using fluorescence and Fourier transform infrared spectroscopy, electrophoresis techniques, chromatographic analysis, and confocal microscopy, we investigated the effects of FA in the early stages of A$\beta$ fibrillogenesis in vitro. Our results show that FA interacts promptly with A$\beta$ monomers/oligomers, interfering since the beginning with its self-assembly and finally forming amorphous aggregates more prone to destabilization. These findings highlight the molecular basis underlying FA antiamyloidogenic activity in AD. © 2013 American Chemical Society.