Inhibition of Protein Aggregation by Several Antioxidants

Oxidative Medicine and Cellular Longevity
Samra HasanbašićEva Zerovnik

Abstract

Amyloid fibril formation is a shared property of all proteins; therefore, model proteins can be used to study this process. We measured protein aggregation of the model amyloid-forming protein stefin B in the presence and absence of several antioxidants. Amyloid fibril formation by stefin B was routinely induced at pH 5 and 10% TFE, at room temperature. The effects of antioxidants NAC, vitamin C, vitamin E, and the three polyphenols resveratrol, quercetin, and curcumin on the kinetics of fibril formation were followed using ThT fluorescence. Concomitantly, the morphology and amount of the aggregates and fibrils were checked by transmission electron microscopy (TEM). The concentration of the antioxidants was varied, and it was observed that different modes of action apply at low or high concentrations relative to the binding constant. In order to obtain more insight into the possible mode of binding, docking of NAC, vitamin C, and all three polyphenols was done to the monomeric form of stefin B.

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Citations

Dec 14, 2019·Scientific Reports·Filippa Lo CascioRakez Kayed
Aug 2, 2020·The Journal of Biological Chemistry·Filippa Lo CascioRakez Kayed
Jun 3, 2021·Biology·Katsuya IuchiHisashi Hisatomi

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Methods Mentioned

BETA
electrophoresis
Fluorescence
circular
circular dichroism
electrophoretic techniques
X-ray

Software Mentioned

JSmol
SwissDock
EADock DSS
DigitalMicrograph
Databank

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