In vitro anti-inflammatory, in silico molecular docking and molecular dynamics simulation of oleanane-type triterpenes from aerial parts of Mussaenda recurvata. Issue 8 (13th February 2023)

• Record Type: Journal Article
• Authors: Tri, Mai Dinh; Phat, Nguyen Tan; Minh, Phan Nhat; Chi, Mai Thanh; Hao, Bui Xuan; Minh An, Tran Nguyen; Alam, Mahboob; Van Kieu, Nguyen; Dang, Van-Son; Mai, Tran Thi Ngoc; Duong, Thuc-Huy
• Is Part Of: RSC advances. Volume 13:Issue 8(2023)
• Page Start: 5324
• Page End: 5336
• Publication Date: 2023-02-13
• Subjects: Chemistry -- Periodicals; 540.5
• DOI: 10.1039/d2ra06870b
• Languages: English
• ISSNs: 2046-2069

Abstract

Abstract : Two new triterpenes recurvatanes A and B were isolated from Mussaenda recurvata using bioactive-guided investigation. Abstract : Bioactive-guided investigation of the aerial parts of Mussaenda recurvata Naiki, Tagane, and Yahara (Rubiaceae) led to the isolation of four triterpenes, including two new triterpenes recurvatanes A and B (1 and 2 ), along with two known compounds 3β, 6β, 23-trihydroxyolean-12-en-28-oic acid (3 ) and 3β, 6β, 19α, 23-tetrahydroxyolean-12-en-28-oic acid (4 ). The chemical structures of the compounds were identified from spectroscopic data and by comparison with the literature. A comprehensive review of NMR data of the oleanane-type triterpenes bearing 3-hydroxy and 4-hydroxymethylene groups indicated the characteristic spectroscopic features in this series. Compounds 1–4 were evaluated for the inhibitory NO production in LPS-stimulated RAW264.7 cells. Compounds 2 and 3 showed a moderate reduction of nitrite accumulation with IC50 values of 55.63 ± 2.52 and 60.08 ± 3.17 μM, respectively. Molecular docking model dedicated to compound 3 or pose 420, which is the best candidate among docking poses of compounds 1–4 interacted well with the crystal structure of enzyme ; 4WCU : PDB. The best ligand molecule, pose 420 in terms of binding energy obtained from docking studies on molecular dynamics (MD) simulations for 100 ns exhibited non-bonding interactions with the protein and remained stable inside the active site.