Triterpenoids with inhibitory effects on lipid accumulation from Ganoderma lucidum
Related Experiment Video
Updated: May 17, 2025

Isolation and Purification of Fungal β-Glucan as an Immunotherapy Strategy for Glioblastoma
Published on: June 2, 2023
Lu Chai1, Xiao-Cui Liu1, Zhou-Wei Wu1
1State Key Laboratory of Phytochemistry and Natural Medicines, Kunming Institute of Botany, Chinese Academy of Sciences, Kunming 650201, Yunnan, People's Republic of China; University of Chinese Academy of Sciences, Beijing 100049, People's Republic of China.
Abstract:
Eight undescribed lanostane-type triterpenes (1-8) and twenty-seven known analogues (9-35) were isolated from the fruiting bodies of cultivated Ganoderma lucidum. The chemical structures of these compounds were elucidated using a combination of spectroscopic techniques. Ganosinenic acid D (1) and ganosinenic acid E (2) were identified as rare pentacyclic triterpenoids with an unusual four-membered carbon ring motif. The inhibitory effects of all compounds on lipid accumulation were evaluated in oleic acid (OA)-induced HepG2 cells. Among the tested compounds, ganolucidic acid G (7), lucidenic acid N (9), methyl lucidenate M (29) showed moderate inhibitory effects. Furthermore, lucidenic acid N inhibited lipid accumulation in a dose-dependent manner. The structure-activity relationship analysis revealed enhanced efficacy in side chain-degraded C27 nor-triterpenoids compared to C24 and C30 analogs.
More Related Videos
Related Concept Videos
Lipid-Lowering Drugs: Statins and Miscellaneous Agents
Enzyme Inhibition
Dipeptidyl Peptidase 4 Inhibitors
Indirect-Acting Cholinergic Agonists: Chemistry and Structure-Activity Relationship
Reversible inhibitors display short to medium durations of action. Short-acting agents include simple alcohols with...
Oral Hypoglycemic Agents: α-Glucosidase Inhibitors
Acarbose and miglitol are...
Indirect-Acting Cholinergic Agonists: Mechanism of Action
Reversible inhibitors like edrophonium bind to a specific part of the enzyme called the anionic catalytic site. They form noncovalent bonds, which means they are not strongly attached to the enzyme. This creates a temporary and less stable enzyme–inhibitor complex,...

