Protective Ability of Perovskia abrotanoides Karel Root Extract on the Aggregation of Protein In Vitro

Background: Protein misfolding can lead to aggregation and these protein aggregates are a fundamental cause of many neurodegenerative disorders such as Alzheimer's, Parkinson's, Huntington's, Prion disease and amyotrophic lateral sclerosis. In recent years, a wide variety of natural compounds have been investigated as protein aggregation inhibitors. Many investigations have reported the therapeutic effects of botanicals constituents and their derivatives in neurodegenerative diseases. Objective: In this study, we examined the effect of Perovskia abrotanoides Karel (P. abrotanoides) root extract on the 1,4-dithiothreitol (DTT)-induced aggregation of proteins. Methods: The anti-aggregation ability of P. abrotanoides root extract was studied using visible absorption spectroscopy (light scattering), fluorescence spectroscopy, and circular dichroism (CD) spectroscopy. Result: The protective effect of P. abrotanoides root extract was varied in the three different-sized proteins (insulin, α-lactalbumin, and ovotransferrin). Conclusion: The results showed that P. abrotanoides root extract was able to inhibit protein aggregations in a concentration-dependent manner due to the interaction of P. abrotanoides root extract with hydrophobic area of proteins.