An In Vitro elucidation of the antiaggregatory potential of Diosminover thermally induced unfolding of hen egg white lysozyme; A preventive quest for lysozyme amyloidosis

International Journal of Biological Macromolecules
Mohammad FurkanRizwan Hasan Khan

Abstract

Protein misfolding diseases are associated with human pathologies. These neurodegenerative diseases remain challenging task for researchers because of their adverse effect on vital organs system. Lysozyme amyloidosis is also associated with multi-organ dysfunction. Hence elucidation of its folding pathway is of great importance, for which hen egg white lysozyme (HEWL) being homological to its human counterpart was taken into consideration. Here in this study we have investigated the effect of diosmin (DSN), a flavonoid over thermally aggregated HEWL. Decrease in ANS, ThT and Rayleigh scattering fluorescence intensity suggests the transition between β to α conformations. Further decrease in absorbance at 360 nm and of congo red with slight blue shift also indicated the disappearance of β sheeted structure under the under the influence of increasing concentration of DSN. These results were also supported by circular dichroism in which gradual appearance α helical structure was observed. Finally visualization under transmission electron microscopy (TEM) authenticated the maximum structural alteration in the previously formed aggregates of HEWL at 250 μM DSN. Molecular docking followed by 100 ns MD simulations help to understand th...Continue Reading

Citations

Mar 7, 2020·Journal of Biomolecular Structure & Dynamics·Zeyaul IslamPrasanna R Kolatkar
Jan 4, 2020·International Journal of Biological Macromolecules·Vanessa T R KiralyJúlio C Borges
May 28, 2019·International Journal of Biological Macromolecules·Mohammad FurkanRizwan Hasan Khan
Jun 8, 2021·International Journal of Biological Macromolecules·Hossein AshrafianRizwan Hassan Khan

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