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Nanobiocatalyst facilitated aglycosidic quercetin as a potent inhibitor of tau protein aggregation.
Kumar, Sanjay; Krishnakumar, V Guru; Morya, Vinod; Gupta, Sharad; Datta, Bhaskar.
Afiliación
  • Kumar S; Department of Biological Engineering, Indian Institute of Technology, Gandhinagar, Gujarat, India.
  • Krishnakumar VG; Department of Biological Engineering, Indian Institute of Technology, Gandhinagar, Gujarat, India.
  • Morya V; Department of Biological Engineering, Indian Institute of Technology, Gandhinagar, Gujarat, India.
  • Gupta S; Department of Biological Engineering, Indian Institute of Technology, Gandhinagar, Gujarat, India.
  • Datta B; Department of Biological Engineering, Indian Institute of Technology, Gandhinagar, Gujarat, India; Department of Chemistry, Indian Institute of Technology, Gandhinagar, Gujarat, India. Electronic address: bdatta@iitgn.ac.in.
Int J Biol Macromol ; 138: 168-180, 2019 Oct 01.
Article en En | MEDLINE | ID: mdl-31306707
Polyphenols have been suggested as potential therapeutic agents for the treatment of amyloidogenic diseases. In this work, we evaluate quercetin-rich onion extract for its ability to inhibit tau fibrillization. Considering the presence of polyphenols in multiple glycosidic and aglycosidic forms, a nanobiocatalyst-mediated approach has been used to extract quercetin from onion skins. The nanobiocatalysts facilitate greater release of quercetin compared to the use of free enzymes. Atomic force microscopy and fluorescence microscopy show that quercetin possesses a novel inhibitory character on tau-fibril aggregation. In contrast, quercetin-diglucoside does not have an inhibitory effect. Molecular Dynamics simulations reveal conformational changes in tau protein upon interaction with quercetin due to specific hydrogen bonding and hydrophobic interactions. The resulting conformational stability of tau monomer reduces propensity of the protein to aggregate. The ability of quercetin to inhibit tau fibrillization expands the paradigm for application of bioactive polyphenols.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Quercetina / Proteínas tau / Nanoestructuras / Enzimas Inmovilizadas / Nanopartículas / Biocatálisis / Agregado de Proteínas Idioma: En Revista: Int J Biol Macromol Año: 2019 Tipo del documento: Article País de afiliación: India Pais de publicación: Países Bajos
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Quercetina / Proteínas tau / Nanoestructuras / Enzimas Inmovilizadas / Nanopartículas / Biocatálisis / Agregado de Proteínas Idioma: En Revista: Int J Biol Macromol Año: 2019 Tipo del documento: Article País de afiliación: India Pais de publicación: Países Bajos