Tamarixetin 3‑O‑β‑d‑Glucopyranoside from Azadirachta indica Leaves: Gastroprotective Role through Inhibition of Matrix Metalloproteinase‑9 Activity in Mice

Neem (Azadirachta indica) is a well-known medicinal and insecticidal plant. Although previous studies have reported the antiulcer activity of neem leaf extract, the lead compound is still unidentified. The present study reports tamarixetin 3-O-β-d-glucopyranoside (1) from a methanol extract of neem...

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Published inJournal of natural products (Washington, D.C.) Vol. 80; no. 5; pp. 1347 - 1353
Main Authors Yadav, Dharmendra K, Bharitkar, Yogesh P, Hazra, Abhijit, Pal, Uttam, Verma, Sugreev, Jana, Sayantan, Singh, Umesh P, Maiti, Nakul C, Mondal, Nirup B, Swarnakar, Snehasikta
Format Journal Article
LanguageEnglish
Published United States American Chemical Society and American Society of Pharmacognosy 26.05.2017
Subjects
Animals
Anti-Ulcer Agents - chemistry
Anti-Ulcer Agents - pharmacology
Azadirachta - chemistry
Disaccharides - chemistry
Disaccharides - isolation & purification
Disaccharides - pharmacology
Indomethacin - chemistry
Indomethacin - pharmacology
Matrix Metalloproteinase 9 - chemistry
Matrix Metalloproteinase 9 - metabolism
Mice
Molecular Docking Simulation
Molecular Structure
Phytotherapy
Plant Leaves
Quercetin - analogs & derivatives
Quercetin - chemistry
Quercetin - isolation & purification
Quercetin - pharmacology
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Summary:Neem (Azadirachta indica) is a well-known medicinal and insecticidal plant. Although previous studies have reported the antiulcer activity of neem leaf extract, the lead compound is still unidentified. The present study reports tamarixetin 3-O-β-d-glucopyranoside (1) from a methanol extract of neem leaves and its gastroprotective activity in an animal model. Compound 1 showed significant protection against indomethacin-induced gastric ulceration in mice in a dose-dependent manner. Moreover, ex vivo and circular dichroism studies confirmed that 1 inhibited the enzyme matrix metalloproteinase-9 (MMP-9) activity with an IC50 value of ca. 50 μM. Molecular docking and dynamics showed the binding of 1 into the pocket of the active site of MMP-9, forming a coordination complex with the catalytic zinc, thus leading to inhibition of MMP-9 activity.
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ISSN:0163-3864
1520-6025
DOI:10.1021/acs.jnatprod.6b00957