Aberrant protein misfolding and/or aggregation and fibrillation has been linked to the pathogenesis of several debilitating chronic diseases including Alzheimer's and Parkinson's disease. Inhibiting protein amyloidogenesis has been proposed as a viable strategy to prevent or ameliorate associated disorders. Herein, we investigated the anti-amyloidogenic properties of biogenic gold nanoparticles (QTG-GNP) prepared via a simple green chemistry route and stabilized by quercetin-functionalized tara gum (QTG). The synthesized QTG-GNP was extensively characterized for its physicochemical attributes via UV-visible spectroscopy, TEM, FESEM, EDX, DLS/Zeta potential, FTIR, RAMAN, XRD, XPS, and TGA analyses, as well as for its biological properties. The results revealed that small-sized (5.01 ± 1.17 nm), well-dispersed, highly stable and round-shaped biogenic gold nanoparticles were successfully synthesized at room temperature with QTG as the sole reductant /stabilizer. Importantly, QTG-GNP demonstrated potent anti-aggregation and fibrillation inhibitory effects against amyloidogenic hen egg white lysozyme (HEWL). Also, QTG-GNP was able to dissociate pre-formed HEWL amyloid fibrils. Furthermore, the constructed nanoparticles exhibited potent anti-radical activities against DPPH and ABTS+ and were cytocompatible with mouse L929 fibroblast cells. On the basis of these findings, it was established that QTG-GNP holds strong prospects for further development as an agent for countering protein aggregation and associated disease conditions.
Keywords: Alzheimer's disease; Antioxidant activity; Cytocompatibility; Gold nanoparticles; Hen egg white lysozyme; Protein fibrillation.
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