Korean Thistle (Cirsium japonicum var. maackii (Maxim.) Matsum.): A Potential Dietary Supplement against Diabetes and Alzheimer's Disease.

Aditi Wagle,Su Hui Seong,Srijan Shrestha,Hyun Ah Jung,Jae Sue Choi

doi:10.3390/molecules24030649

Aditi Wagle, Su Hui Seong + Show 3 more

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https://doi.org/10.3390/molecules24030649

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Abstract

In the search for natural products having a dual inhibitory action on diabetes and Alzheimer’s disease, this study investigated the activity of different parts of Korean thistle (Cirsium japonicum var. maackii (Maxim.) Matsum), and its fractional constituents by in vitro enzymatic and in silico molecular docking studies. Cirsium maackii has been used as a traditional medicine for the treatment of several diseases. The ethyl acetate and dichloromethane fractions of a leaf extract showed α-glucosidase and BACE1 inhibitory activity, respectively. Furthermore, the isolated compound, luteolin, exhibited concentration-dependent non-competitive inhibition against both α-glucosidase and BACE1 (IC50 = 51.27 ± 1.23 and 13.75 ± 0.26 μM; Ki value = 52.04 and 14.76 μM, respectively). Moreover, docking studies showed that luteolin formed a strong hydrogen bond with the peripheral binding amino acid residues, and hydrophobic interactions with the α-glucosidase and BACE1 enzymes. Therefore, Korean thistle may act as an important dietary supplement against diabetes and Alzheimer’s disease, especially the leaves, because of the preponderance of the active component, luteolin, making Korean thistle a promising candidate for more detailed in vitro and in vivo studies.

Highlights

Diabetes is one of the most common metabolic disorder in today’s world
Our results showed luteolin to have strong human intestinal absorption while glucosides(Table showed absorption
The Ki values can be a useful tool to compare the activity of the compounds, showing the binding affinity of the inhibitor to the enzyme (Table 3). These results suggest that luteolin exhibits the strongest binding affinity for the α-glucosidase and BACE1 enzymes

Summary

Introduction

Diabetes is one of the most common metabolic disorder in today’s world. According to the International Diabetes Federation, 451 million people were affected with diabetes in 2017 and that number might increase to 693 million by the year 2045. It is estimated that nearly half of all the population are undiagnosed with diabetes, which could increase their risk of developing more complications [1]. T2D is to decrease the absorption of carbohydrates from the food we consume. This can be done by inhibiting the carbohydrate-hydrolyzing enzyme α-glucosidase present in the epithelium of the small intestine. Α-Glucosidase, an exo-type carbohydrase enzyme widely distributed in microorganisms, plants, and animal tissues, catalyzes the liberation of α-glucose from the non-reducing end of the substrate [4]. Inhibiting α-glucosidase decreases the rate of hydrolytic cleavage of oligosaccharide, and the process of carbohydrate digestion extends to the lower part of the small intestine, delaying the overall absorption rate of glucose into the blood [5,6]

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