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Issue 50, 2017, Issue in Progress
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Curcumin-like compounds designed to modify amyloid beta peptide aggregation patterns

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Abstract

Curcumin is a natural polyphenol able to bind the amyloid beta peptide, which is related to Alzheimer’s disease, and modify its self-assembly pathway. This paper focuses on a multi-disciplinary study that starts from the design of curcumin-like compounds with the key chemical features required for inhibiting amyloid beta aggregation, and reports the effects of these compounds on the in vitro aggregation of amyloid beta peptides. Chemoinformatic screening was performed through the calculation of molecular descriptors that were able to highlight the drug-like profile, followed by docking studies with an amyloid beta peptide fibril. The computational design underlined two different scaffolds that were easily synthesized in good yields. In vitro experiments, ranging from fluorescence spectroscopy and confocal microscopy up to small angle X-ray scattering, provided evidence that the synthesized compounds are able to modify the aggregation pattern of amyloid beta peptides both in the secondary structures, and in terms of the overall structure dimensions. The cytotoxic potential of the synthesized compounds was finally tested in vitro with a model neuronal cell line (LAN5). The overall view of this study suggests new concepts and potential difficulties in the design of novel drugs against diverse amyloidoses, including Alzheimer’s disease.

Graphical abstract: Curcumin-like compounds designed to modify amyloid beta peptide aggregation patterns

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Publication details

The article was received on 10 May 2017, accepted on 07 Jun 2017 and first published on 21 Jun 2017


Article type: Paper
DOI: 10.1039/C7RA05300B
Citation: RSC Adv., 2017,7, 31714-31724
  • Open access: Creative Commons BY license
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    Curcumin-like compounds designed to modify amyloid beta peptide aggregation patterns

    A. Battisti, A. Palumbo Piccionello, A. Sgarbossa, S. Vilasi, C. Ricci, F. Ghetti, F. Spinozzi, A. Marino Gammazza, V. Giacalone, A. Martorana, A. Lauria, C. Ferrero, D. Bulone, M. R. Mangione, P. L. San Biagio and M. G. Ortore, RSC Adv., 2017, 7, 31714
    DOI: 10.1039/C7RA05300B

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