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Curcumin-Like Compounds as Neuroprotective Agents: Interactions with HSP60 and Amyloid Beta Peptide

  • Autori: PALUMBO PICCIONELLO, A.; MARINO GAMMAZZA, A.; Campanella, C.; Riccobono, A.; Giacalone, V.; Vilasi, S.; Ortore, M.; CARUSO BAVISOTTO, C.; Cappello, F.
  • Anno di pubblicazione: 2014
  • Tipologia: Proceedings (TIPOLOGIA NON ATTIVA)


Alzheimer’s Disease (AD) represents a fundamental challenge for public health in the 21st century. Current AD therapies largely focus on symptomatic aspects of the clinical pathology, but they have yet to demonstrate any major impact on the disease progression [1]. The most important role of the research aimed at fighting the AD is the development of neuro-protective agents, able to interfere with the protein aggregation process whose clinical signature is represented by the plaques deposition. An important role in AD’s framework could be played by Heat shock proteins (HSPs), highly regulated proteins that mediate the proteins proper folding and promote recovery of their native conformations lost due to stress [2]. Recently, it was shown that HSP60 mediates translocation of Amyloid Precursor Protein (APP) and Amyloid Beta peptide (Aβ) to the mitochondria, leading to dysfunction of the organelle [3]. In the field of potential therapeutic approaches, curcumin, a non-toxic component of the curry spice turmeric, with anti-inflammatory, antioxidant and anti-aggregation properties, is emerging as a lead-compound for the development of neuro-protective drugs [4]. Here we present our recent findings on Curcumin and Curcumin-like drugs obtained by a combination of cellular and in-vitro experiments, such as Thioflavine T fluorescence spectroscopy and Small Angle X-ray Scattering [5]. In particular, together with the synthesis of some curcumin-like compounds, we present the results about their effect on a neuronal cell model, concerning the cytotoxicity and ability to affect Hsp60 expression, as well as their influence on Aβ aggregation, provided by in vitro experiments.