PTP1B inhibition studies of biological active phloroglucinols from the rhizomes of Dryopteris crassirhizoma: Kinetic properties and molecular docking simulation

Acetylcholinesterase inhibition studies of alkaloid components from Crinum asiaticum var. sinicum plants: In vitro assessments by molecular docking and molecular dynamics simulations

“…The two main processes in the docking procedure are determining the binding a nity and forecasting ligand shape, location, and orientation in these sites. The advantages of virtual screening include a limited search area, low cost, and high level of exibility, all of which can help rapidly identify an appropriate target protein inhibitor [37]. To explore the interactions and binding of these compounds with AChE activity and to investigate the anti-AChE activity of the most active molecule, a molecular docking study was conducted.…”

Inhibitory Activity of Bioactive Phloroglucinols from the Rhizomes of Dryopteris crassirhizoma on Escherichia coli β-Glucuronidase: Kinetic Analysis and Molecular Docking Studies

“…Among all the isolated compounds, trimeric phloroglucinols ( 26 – 28 ) displayed the strongest inhibitory effect against β -glucuronidase. In vitro assessments revealed that nortrisflavaspidic acid ABB ( 26 ), trisflavaspidic acid ABB ( 27 ), and trisflavaspidic acid BBB ( 28 ), with two butyryl side chains linked to phenol rings in phloroglucinol trimeric structures, significantly exhibited PTP1B [ 23 ]. In this study, these molecules also showed significant β -glucuronidase inhibitory activity with IC 50 values of 8.0 ± 1.8, 7.1 ± 2.6, and 5.6 ± 1.1 µM, respectively, which was more potent than that of the positive control DSA.…”

“…Molecular docking simulations were performed to understand the binding efficiency and interaction of active compounds with β -glucuronidase using AutoDock 4.2 (Scripps Research Institute, La Jolla, CA, USA) [ 32 ], as per our previously described protocol [ 23 , 31 ]. The 3D X-ray crystallographic structure of E .…”

“…The trimeric compounds filixic acid ABA and nortrisflavaspidic acid ABB exhibited a strong inhibitory effect on neuraminidase of influenza virus H5N1, with IC 50 values of 29.6 and 51.5 μM, respectively [ 22 ]. Furthermore, nortrisflavaspidic acid ABB, trisflavaspidic acid ABB, and trisflavaspidic acid BBB are considered promising treatments for type 2 diabetes due to their significant activity toward the PTP1B enzyme [ 23 ]. Although many biological activities of secondary metabolites from the rhizomes of D .…”

“…Based on analysis of various modern spectroscopic data, such as high-resolution mass spectrometry, 1D and 2D nuclear magnetic resonance (NMR), spectroscopy as well as comparison with corresponding results in the literature, the chemical structures of the isolated compounds were identified as 2,4,6-trihydroxy-acetophenone ( 1 ), 1-(2,4,6-trihydroxy-phenyl)-propan-1-one ( 2 ), phlorobutyrophenone ( 3 ), 5-acetyl-2,4,6-trihydroxyacetophenone ( 4 ), 1,3-(2,4,6-trihydroxyphenyl)dipropanone ( 5 ), 1,3-(2,4,6-trihydroxyphenyl)dibutanone ( 6 ), 1-(2,4,6-trihydroxy-3-methylphenyl)propanone ( 7 ), 1-(2, 4, 6-trihydroxy-3-methylphenyl) butanone ( 8 ), 1-(2, 4, 6-trihydroxy-3-methylphenyl) pentanone ( 9 ), tripropionylphloroglucinol ( 10 ), tributyrylphloroglucinol ( 11 ), bis-phlorobutyrophenone ( 12 ), dryopidin PB ( 13 ), methylene-bis-phlorobutyrophenone ( 14 ), araspidin BB ( 15 ), norflavaspidic acid AP ( 16 ), norflavaspidic acid AB ( 17 ), norflavaspidic acid PB ( 18 ), norflavaspidic acid BB ( 19 ), flavaspidic acid AA ( 20 ), flavaspidic acid AP ( 21 ), flavaspidic acid AB ( 22 ), flavaspidic acid PB ( 23 ), albaspidin AA ( 24 ), dryopcrassirine AB ( 25 ), nortrisflavaspidic acid ABB ( 26 ), trisflavaspidic acid ABB ( 27 ), trisflavaspidic acid BBB ( 28 ), filixic acid ABA ( 29 ), and dryocrassin ABBA ( 30 ) ( Figure 1 ). All isolated compounds were evaluated for their PTP1B inhibitory activities through in vitro assays, and some exhibited significant inhibitory effects [ 23 ].…”