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

Abstract

The phytochemical constituents from the roots of Millettia speciosa 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 M. speciosa. Out of the isolated compounds, eight showed inhibitory effects on NO production in lipopolysaccharide (LPS)-stimulated RAW 264.7 cells, with IC50 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, 4, 5, and 10 exhibited excellent α-glucosidase inhibition, with IC50 values ranging from 1.1 to 2.2 µg/mL. Almost all of the test compounds showed little or no acetylcholinesterase inhibition, except for 5, which showed moderate anti-acetylcholinesterase activity in vitro. The molecular docking study of α-glucosidase inhibition by 3–5 and 10 was conducted to observe the interactions of these molecules with the enzyme. Compounds 4, 5, and 10 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 3 and the positive control acarbose. Our findings evidence the pharmacological potential of this species and suggest that the phytochemicals derived from the roots of M. speciosa may be promising lead molecules for further studies on the development of anti-inflammatory and anti-diabetes drugs.

In vitro and in silico docking and molecular dynamic of antimicrobial activities, alpha-glucosidase, and anti-inflammatory activity of compounds from the aerial parts of Mussaenda saigonensis

“…Among 1-12, ursolic acid is believed to be a well-known inhibitor with many published reports. 43,46,47 Biological data of 8-12 gave consistency with those reported previously. [48][49][50] Compound 12 are the best candidate for alpha glucosidase enzyme inhibition among us and positive control, acarbose with the IC 50 value of 42.4 mM.…”

“…Phenylethanoids 11 and 12 have also been reported to be weak NO inhibitors 1 According to the authors, 11 and 12 are both weaker than 4. Other compounds that inhibit NO have previously been reported: 5, 40 6, 41 7, 42 8, 41,42 9, 43,44 and 10. 45…”

Evaluation of Possible Antioxidant, Anti-Hyperglycaemic, Anti-Alzheimer and Anti-Inflammatory Effects of Teucrium polium Aerial Parts (Lamiaceae)

“…The obtained results further consolidated what was previously reported by Dastjerdi et al [ 48 ], showing that Iranian T. polium possesses a very good activity in α-amylase inhibitory assay with IC 50 values of 3.01 and 1.64 mg/mL for the dichloromethane extract and with ethyl acetate extracts, respectively. Flavonoids elicited an antihyperglycemic effect via suppressing α-glucosidase and α-amylase activities, attenuating insulin resistance and promoting pancreatic cell proliferation [ 5 , 49 ]. Moreover, many studies further supported the results of in silico studies, where luteolin revealed a potent antihyperglycemic effect via inhibition of α-amylase [ 50 ].…”

Antimicrobial, Cytotoxic, and α-Glucosidase Inhibitory Activities of Ethanol Extract and Chemical Constituents Isolated from Homotrigona apicalis Propolis—In Vitro and Molecular Docking Studies

“…As the structure of α -glucosidase of Saccharomyces cerevisiae was not available in the RCSB database, a homology model was employed using the isomaltase of S. cerevisiae as the template (PDB ID: 3AJ7). In this study, the homology model was generated and evaluated using the Swiss-Model server, following the protocol described by Nguyen Ngoc Tuan et al [ 28 ]. After removing the water molecules, hydrogen atoms were added, and partial charges were assigned using Autodock Tool 1.5.6 software.…”