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

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Author(s): Seyed Mahmoud Puormand, Arezou Ghahghaei*, Jafar Valizadeh, Shahrzad Nazari.

Journal Name: The Natural Products Journal

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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. 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. The anti-aggregation ability of P. abrotanoides root extract was studied using visible absorption spectroscopy (light scattering), fluorescence spectroscopy, and circular dichroism (CD) spectroscopy. The protective effect of P. abrotanoides root extract was varied in the three different-sized proteins (insulin, α-lactalbumin, and ovotransferrin). 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.

Keywords: P. abrotanoides Karel. misfolding. aggregation. neurodegenerative disorders, Light Scattering, Circular Dichroism spectroscopy

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(E-pub Ahead of Print)
DOI: 10.2174/2210315509666190425125312
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