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Chromones and biflavonoids from Garcinia pedunculata and Garcinia nujiangensis and their anti-inflammatory activity.

Authors :
Fan X
Guo J
Feng D
Li D
Hua H
Source :
Phytochemistry [Phytochemistry] 2024 Aug; Vol. 224, pp. 114166. Date of Electronic Publication: 2024 May 27.
Publication Year :
2024

Abstract

Plants of the Garcinia genus were rich in structurally diverse and naturally bioactive components, while limited studies have been reported for Garcinia pedunculata Roxb. and G. nujiangensis C. Y. Wu & Y. H. Li. Four previously undescribed compounds including three chromones, garpedunchromones A-C (1-3), and one biflavonoid, nujiangbiflavone A (14), along with fifteen known analogs (4-13, 15-19) were isolated from G. pedunculata and G. nujiangensis. The structures of the isolated compounds were determined based on their HRESIMS data, extensive NMR spectroscopic analyses, and ECD calculations. The chromone derivatives were isolated from Garcinia for the first time. Compound 14 was a rare biflavonoid with C-3─C-6″ linkage. The biological evaluation of these isolates against NO production was conducted in the LPS-induced RAW 264.7 cells, resulting in the identification of a series of potent NO inhibitors, of which garpedunchromone B (2) was the most active with an IC <subscript>50</subscript> value of 18.11 ± 0.96 μM. In the network pharmacology studies, the potential targets of compounds and inflammation were obtained from PharmMapper and GeneCards database. GO and KEGG enrichment analysis revealed that the overlapped targets were closely related to the major pathogenic processes linked to inflammation. Garpedunchromone B and proteins binding sites were being predicted.<br />Competing Interests: Declaration of competing interest The authors confirm that this research article has no conflict of interest. Four chromones and fifteen flavonoids including four previously undescribed compounds were isolated from Garcinia pedunculata and G. nujiangensis. Compound 2 exhibited significant activity in inhibiting NO release, and the protein binding site was predicted.<br /> (Copyright © 2024 Elsevier Ltd. All rights reserved.)

Details

Language :
English
ISSN :
1873-3700
Volume :
224
Database :
MEDLINE
Journal :
Phytochemistry
Publication Type :
Academic Journal
Accession number :
38810815
Full Text :
https://doi.org/10.1016/j.phytochem.2024.114166