Evidence map›Paper›PMID 42432862›Full record

ArticleLuminescence : the journal of biological and chemical luminescence2026

Inhibition of Oroxyloside Against Two Sources of α-Amylase/α-Glucosidase: Spectral Analysis, Computer Simulation, and mm-PBSA Calculation.

Yuan Li, Suqing Wang, Yutong Du, Di Lian, Jingjing Cui, Xue Zhang, Zihan Qu, Li Li

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In one paragraph

Article in Luminescence : the journal of biological and chemical luminescence, 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

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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

8 authors.

Yuan LiThe College of Chemistry, Changchun Normal University, Changchun, China.
Suqing WangThe College of Chemistry, Changchun Normal University, Changchun, China.
Yutong DuThe College of Chemistry, Changchun Normal University, Changchun, China.
Di LianThe College of Chemistry, Changchun Normal University, Changchun, China.
Jingjing CuiThe College of Chemistry, Changchun Normal University, Changchun, China.
Xue ZhangThe College of Chemistry, Changchun Normal University, Changchun, China.
Zihan QuThe College of Chemistry, Changchun Normal University, Changchun, China.
Li LiThe College of Chemistry, Changchun Normal University, Changchun, China.ORCID https://orcid.org/0000-0003-3971-7896

Funding

Jilin Provincial Natural Science Foundation YDZJ202601ZYTS377
6 · The paper itself

Abstract

In this work, the inhibition effects of oroxyloside on two α-amylase from porcine pancreas (PPA) and Bacillus subtilis (BSA), as well as two α-glucosidase from Aspergillus niger (ANG) and Saccharomyces cerevisiae (SCG), were systematically compared using spectral analysis, computer simulation, and mm-PBSA calculation. Oroxyloside displayed the most potent inhibitory activity on ANG, followed by PPA, BSA, and SCG. Meanwhile, oroxyloside exhibited a mixed-type inhibition against BSA, PPA, ANG, and SCG. Oroxyloside interacted with enzyme residues mainly by hydrogen bonds and van der Waals forces, leading to the changes in the microenvironment and the secondary structure changes of enzymes, and ultimately exerting inhibitory effects. The optimal binding modes and the stability of four complexes were predicted by computer simulation. The free energy decomposition of critical residues was calculated using mm-PBSA. Oroxyloside was identified as a potential inhibitor of four enzymes, exhibiting significantly stronger inhibitory activity than acarbose.

Indexed as

alpha-Amylasesalpha-GlucosidasesEnzyme InhibitorsFlavonoidsGlycoside Hydrolase InhibitorsAnimalsAspergillus nigerComputer SimulationMolecular StructureSaccharomyces cerevisiaeSwine5,7-dihydroxy-6-methoxy-2-phenylchromen-4-onealpha-Amylasesalpha-GlucosidasesEnzyme InhibitorsFlavonoidsGlycoside Hydrolase Inhibitorscomputer simulationmm‐PBSAoroxylosidespectral analysisα‐amylaseα‐glucosidase

Identifiers

PMID42432862
PMCPMC13354827

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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.