Effective suppression of the modified PHF6 peptide/1N4R Tau amyloid aggregation by intact curcumin, not its degradation products: Another evidence for the pigment as preventive/therapeutic "functional food"

International Journal of Biological Macromolecules
Nooshin BijariReza Khodarahmi

Abstract

Curcumin is a natural product with multiple biological activities and numerous potential therapeutic applications. In present study, the influence of curcumin and its degradation products (DPs) on the amyloid aggregation of Tau protein and the related PHF6 peptide were investigated. We provided experimental/theoretical evidence for suppressing effects of the compounds on the amyloid formation using far-UV CD as well as AFM, XRD and docking techniques and showed that the parent curcumin displayed stronger inhibition effect against Tau fibril aggregation. The obtained results suggest that the curcumin/DPs binding sites on the Tau molecule are likely to be the same, and provide a good structural basis to explain the efficient aggregation suppressing behavior of the curcumin, compared to the DPs. So, developing more stable curcumin nanoparticle formulations with improved curcumin bioavailability are of great importance. Curcumin's multi-functionality is also highly significant for the therapeutic application of this natural compound against various human diseases.

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Citations

Jan 25, 2020·International Journal of Molecular Sciences·Varnavas D MouchlisAntreas Afantitis
Apr 15, 2020·Current Pharmaceutical Design·Kadja Luana Chagas MonteiroEdeildo Ferreira da Silva-Júnior
Jun 27, 2019·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Qiuchen ZhengNoel D Lazo
Dec 6, 2019·Archives of Biochemistry and Biophysics·Vali AkbariReza Khodarahmi
Dec 8, 2020·Frontiers in Neurology·Sebastian S OakleyLouise C Serpell
Dec 22, 2020·Frontiers in Molecular Neuroscience·Yoshiyuki Soeda, Akihiko Takashima
May 9, 2021·Biophysical Chemistry·Marjan MotieiMohammad Hossein Nasr-Esfahani

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