Inhibition of α-Glucosidase, Acetylcholinesterase, and Nitric Oxide Production by Phytochemicals Isolated from Millettia speciosa -In Vitro and Molecular Docking Studies

• Published in: Plants (Basel) 2022-01, Vol.11 (3), p.388
• Main Authors: Tuan, Nguyen Ngoc, Thi, Huong Nguyen, My, Chau Le Thi, Hai, Tang Xuan, Trung, Hieu Tran, Kim, Anh Nguyen Thi, Tan, Thanh Nguyen, Van, Tan Le, Nguyen, Cuong Quoc, Tran, Quang De, Kuo, Ping-Chung, Dang, Quang Le, Thang, Tran Dinh
• Format: Article
• Language: English
• Subjects: Acarbose; Acetylcholinesterase; Acids; anti-acetylcholinesterase; anti-glucosidase; Cytokines; Diabetes mellitus; Drug development; Flavonoids; Glucose; Glucosidase; Inflammation; Lipopolysaccharides; Medical research; Metabolites; Millettia speciosa; Molecular docking; Nitric oxide; NMR; NO production; Nuclear magnetic resonance; Phenolic compounds; Phenols; Phytochemicals; Roots; Triterpenes; Triterpenoids; α-Glucosidase
• ISSN: 2223-7747; 2223-7747
• DOI: 10.3390/plants11030388

The phytochemical constituents from the roots of were investigated by chromatographic isolation, and their chemical structures were characterized using the MS and NMR spectroscopic methods. A total of 10 compounds, including six triterpenoids, two flavonoids, and two phenolic compounds, were identified from the roots of . Out of the isolated compounds, eight showed inhibitory effects on NO production in lipopolysaccharide (LPS)-stimulated RAW 264.7 cells, with IC values ranging from 43.9 to 449.5 µg/mL. Ursane-type triterpenes significantly suppressed NO production compared to the remaining compounds. In addition, these compounds also exhibited remarkable inhibitory effects on α-glucosidase. Among the tested compounds, , , and exhibited excellent α-glucosidase inhibition, with IC values ranging from 1.1 to 2.2 µg/mL. Almost all of the test compounds showed little or no acetylcholinesterase inhibition, except for which showed moderate anti-acetylcholinesterase activity in vitro. The molecular docking study of α-glucosidase inhibition by - and was conducted to observe the interactions of these molecules with the enzyme. Compounds , , and exhibited a better binding affinity toward the targeted receptor and the H-bond interactions located at the entrance of the enzyme active site pocket in comparison to those of and the positive control acarbose. Our findings evidence the pharmacological potential of this species and suggest that the phytochemicals derived from the roots of may be promising lead molecules for further studies on the development of anti-inflammatory and anti-diabetes drugs.