Evidence map›Paper›PMID 42561132›Full record

ArticleChemistry & biodiversity2026

Salicifoliosides A and B: A Pair of Furan Glycoside Isomers From Chimonanthus salicifolius and Their Modulation of the Functions of Caco-2 Cells.

Hui-Zhen Yang, Yi-Wei Wu, Wen-Jie Shangguan, Rui Min, Wen-Ting Zhang, Long Chen, Ke Yang, Tun-Hai Xu, Yin-Di Zhu, Xin-Rong Fan

Abstract read
In one paragraph

Article in Chemistry & biodiversity, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors.

Hui-Zhen YangSchool of Chinese Pharmacy, Beijing University of Chinese Medicine, Beijing, China.ORCID https://orcid.org/0009-0003-5407-1795
Yi-Wei WuSchool of Chinese Pharmacy, Beijing University of Chinese Medicine, Beijing, China.
Wen-Jie ShangguanSchool of Chinese Pharmacy, Beijing University of Chinese Medicine, Beijing, China.
Rui MinSchool of Chinese Pharmacy, Beijing University of Chinese Medicine, Beijing, China.
Wen-Ting ZhangSchool of Chinese Medicine, Wenzhou Medical University, Wenzhou, China.
Long ChenSchool of Chinese Medicine, Wenzhou Medical University, Wenzhou, China.
Ke YangSchool of Life Sciences, China Jiliang University, Hangzhou, China.ORCID https://orcid.org/0009-0000-4109-622X
Tun-Hai XuSchool of Chinese Pharmacy, Beijing University of Chinese Medicine, Beijing, China.
Yin-Di ZhuSchool of Chinese Medicine, Wenzhou Medical University, Wenzhou, China.ORCID https://orcid.org/0009-0007-1040-1261
Xin-Rong FanDepartment of Drug Preparation, Lishui Hospital of Traditional Chinese Medicine Affiliated to Zhejiang Chinese Medical University, Lishui, Zhejiang, China.ORCID https://orcid.org/0009-0006-4445-1518

Funding

Wenzhou Key Laboratory of Research and Translation of Bioactive Components in Traditional Chinese MedicineZhejiang Province Traditional Chinese Medicine Science and Technology Plan Project 2024ZR205
6 · The paper itself

Abstract

Chimonanthus salicifolius has traditionally been used for the treatment of gastrointestinal disorders. In this study, a systematic phytochemical investigation of this plant was conducted, leading to the isolation and identification of two previously undescribed furan glycosides, salicifoliosides A (1) and B (2). Structurally, these compounds feature a rare structural motif consisting of an α,β-unsaturated furanone aglycone esterified with a p-coumaroyl unit, a combination scarcely reported in natural products. Spectroscopic and chemical analyses established that 1 and 2 are cis-trans geometric isomers, offering a unique framework to investigate configuration-dependent properties and expanding the structural diversity of furan glycosides. To evaluate their potential relevance to functional dyspepsia (FD), we adopted a prediction‑to‑validation strategy. Network pharmacology analysis and molecular docking identified matrix metalloproteinase-2 (MMP2) as a potential target. In a lipopolysaccharide (LPS)-stimulated Caco‑2 cell model, compounds 1 and 2 significantly inhibited the secretion of MMP2 and tumor necrosis factor-α (TNF-α), consistent with the earlier in silico predictions. Notably, compound 1 also reduced interleukin-2 (IL-2) levels, suggesting a configuration-dependent effect. This study highlights a previously unrecognized natural product scaffold and provides initial evidence linking its structure to anti-inflammatory activity, offering new insights into structure-activity relationship studies and drug discovery.

Indexed as

FuransGlycosidesCaco-2 CellsDose-Response Relationship, DrugHumansIsomerismLipopolysaccharidesMatrix Metalloproteinase 2Molecular Docking SimulationMolecular StructureStructure-Activity RelationshipTumor Necrosis Factor-alphaFuransGlycosidesLipopolysaccharidesMatrix Metalloproteinase 2Tumor Necrosis Factor-alphaanti‐inflammatoryChimonanthus salicifolius S. Y. Hucis–trans isomersfuran glycosidessalicifolioside

Identifiers

PMID42561132
PMCPMC13446847

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.