Insights into the remarkable attenuation of hen egg white lysozyme amyloid fibril formation mediated by biogenic gold nanoparticles stabilized by quercetin-functionalized tara gum
1
Issued Date
2023-03-31
Resource Type
ISSN
01418130
eISSN
18790003
Scopus ID
2-s2.0-85147209434
Pubmed ID
36586653
Journal Title
International Journal of Biological Macromolecules
Volume
232
Rights Holder(s)
SCOPUS
Bibliographic Citation
International Journal of Biological Macromolecules Vol.232 (2023)
Suggested Citation
Eze F.N., Eze R.C., Ovatlarnporn C. Insights into the remarkable attenuation of hen egg white lysozyme amyloid fibril formation mediated by biogenic gold nanoparticles stabilized by quercetin-functionalized tara gum. International Journal of Biological Macromolecules Vol.232 (2023). doi:10.1016/j.ijbiomac.2022.12.263 Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/81620
Title
Insights into the remarkable attenuation of hen egg white lysozyme amyloid fibril formation mediated by biogenic gold nanoparticles stabilized by quercetin-functionalized tara gum
Author(s)
Other Contributor(s)
Abstract
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[rad] and ABTS[rad]+ 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.