Scientific Results

ß-amyloid amorphous aggregates induced by the small natural molecule ferulic acid

Year: 2013

Authors: Bramanti E., Fulgentini L., Bizzarri R., Lenci F., Sgarbossa A.

Autors Affiliation: Istituto Dei Composti Organo-Metallici, CNR, U.O. Pisa, Via G. Moruzzi, 1, 56124, Pisa, Italy; Istituto di Biofisica, CNR, U.O. Pisa, Via G. Moruzzi, 1, 56124, Pisa, Italy; Istituto Nazionale di Ottica, CNR, U.O. Pisa, Via G. Moruzzi, 1, 56124, Pisa, Italy

Abstract: 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 (Aß) 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 Aß fibrillogenesis in vitro. Our results show that FA interacts promptly with Aß 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.

Journal/Review: JOURNAL OF PHYSICAL CHEMISTRY B

Volume: 117 (44)      Pages from: 13816  to: 13821

More Information: The present work was supported by a Grant from the Italian Ministry of University and Scientific Research for Programs of Relevant National Interest (PRIN 2008-prot.20083Y34Y7) \”Development of a molecular strategy for the prevention of protein aggregation and fibrillogenesis: a biophysical approach\”.

KeyWords: FIBRILS IN-VITRO; ALZHEIMERS-DISEASE; THIOFLAVIN-T; CROSS-LINKING; A-BETA; PROTEIN; BINDING; OLIGOMERS; FIBRILLOGENESIS; NEUROTOXICITY

DOI: 10.1021/jp4079986

Citations: 14
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English