Antimicrobial and alpha-glucosidase inhibitory flavonoid glycosides from the plant Mussaenda recurvata : in vitro and in silico approaches

• Published in: RSC advances Vol. 14; no. 13; pp. 9326 - 9338
• Main Authors: Ngoc Mai, Tran Thi, Minh, Phan Nhat, Phat, Nguyen Tan, Duong, Thuc Huy, Minh An, Tran Nguyen, Dang, Van Son, Van Hue, Nguyen, Tri, Mai Dinh
• Format: Journal Article
• Language: English
• Published: England Royal Society of Chemistry 14-03-2024; The Royal Society of Chemistry
• Subjects: Amino acids; Bacteria; Chemical compounds; Chemistry; Enzymes; Flavone glycosides; Flavonoids; Fungi; Glucosidase; Molecular docking; Molecular dynamics; Pseudomonas aeruginosa; Staphylococcus infections
• ISSN: 2046-2069; 2046-2069
• DOI: 10.1039/d4ra00666f

Seven flavonoid glycosides were isolated from the aerial portions of
during a phytochemical analysis. This comprised one novel component, ecurvoside, and six well-studied compounds, namely astragalin, isoquercitrin, nicotiflorin, rutin, hesperidin, and neohesperidin. The chemical structures of compounds were identified using spectroscopic techniques and a comparison with previously published studies. Alpha-glucosidase inhibition testing was carried out on all isolated compounds. The compounds evaluated have IC
values between 35.6 and 239.1 g mL
, indicating a moderate degree of inhibition.
antimicrobial activities of compounds 1-7 have screened against the bacteria
(
), methicillin-resistant
(MRSA),
(
), and fungi:
(
),
(
), and
(
), where compound 6 showed excellent activity against fungi
with an MIC value of 12.5 μM. In accordance with the molecular docking study, ecurvoside (1) or pose 472 interacted well with the 3TOP enzyme: PDB and the molecular dynamic simulations proved that the complex of ecurvoside and 3TOP has a stable simulation time of 50-100 ns and the significant residual amino acids in 3TOP are relative to interactions more than one time such as Asp 960, Glu 961, Lys 1088, Glu 1095, Arg 1097, Gly 1102, Thr 1103, Gln 1109, Glu 1178: A chain and Glu 1095, Thr 1101, and Asp 1107: B chain. The docking studies of compounds 1-7 to the enzyme 2VF5 explain the general mechanism to inhibit bacteria and proved that compound 6 (pose 370) inhibited stronger than compound 7 (pose 362) and compound 5 (pose 280), and compounds 1 to 4 do not interact well with 2VF5.