ß-amyloid amorphous aggregates induced by the small natural molecule ferulic acid
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/jp4079986Citations: 15data from “WEB OF SCIENCE” (of Thomson Reuters) are update at: 2020-08-09References taken from IsiWeb of Knowledge: (subscribers only)Connecting to view paper tab on IsiWeb: Click hereConnecting to view citations from IsiWeb: Click here