Evidence map›Paper›PMID 42279759›Full record

ArticleFoods (Basel, Switzerland)2026

Molecular Basis for the Divergent Inhibition of α-Amylase and α-Glucosidase by Phenolic Acids: The Critical Role of Hydroxyl Substitution.

Shuang Yang, Yongxing Li, Weiyu Han, Wenhao Cao, Zhihui Hu, Zhangliang Zhu, Mei Li, Jianhui Feng, Jinfang Zhang

Abstract read
In one paragraph

Article in Foods (Basel, Switzerland), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Article
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

9 authors.

Shuang YangSchool of Food Engineering, Ludong University, Yantai 264025, China.
Yongxing LiCenter for Mitochondria and Healthy Aging, College of Life Sciences, Yantai University, Yantai 264005, China.ORCID 0009-0007-4092-5912
Weiyu HanCenter for Mitochondria and Healthy Aging, College of Life Sciences, Yantai University, Yantai 264005, China.
Wenhao CaoCenter for Mitochondria and Healthy Aging, College of Life Sciences, Yantai University, Yantai 264005, China.
Zhihui HuCenter for Mitochondria and Healthy Aging, College of Life Sciences, Yantai University, Yantai 264005, China.
Zhangliang ZhuGraduate School of Biostudies, Kyoto University, Kyoto 606-8501, Japan.
Mei LiCenter for Mitochondria and Healthy Aging, College of Life Sciences, Yantai University, Yantai 264005, China.ORCID 0000-0002-6702-6286
Jianhui FengCenter for Mitochondria and Healthy Aging, College of Life Sciences, Yantai University, Yantai 264005, China.
Jinfang ZhangSchool of Food Engineering, Ludong University, Yantai 264025, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The global rise in metabolic disorders demands novel interventions targeting starch digestion. This study investigated two dietary phenolic acids (caffeic acid (CA) and p-hydroxycinnamic acid (p-HA)) as inhibitors of α-amylase and α-glucosidase through integrated experimental and computational approaches. Molecular docking showed distinct binding modes, and CA formed stable hydrogen bonds with catalytic residues of α-glucosidase, while p-HA interacted mainly with α-amylase via hydrophobic contacts. Enzyme kinetics revealed concentration-dependent mixed-type inhibition, with CA being more potent against α-glucosidase and p-HA against α-amylase. Spectroscopic analysis indicated both acids induced structural changes in the enzymes, with CA causing greater α-helix reduction (Δ7.03% vs. Δ2.10%) by altering the tryptophan microenvironment. Moreover, both compounds significantly suppress glucose absorption in the proximal small intestine in an ex vivo everted gut sac model, with p-HA exhibiting exceptional efficacy in the duodenum. These findings clarify structure-activity relationships and support the potential use of CA and p-HA as local intestinal agents for modulating carbohydrate absorption.

Indexed as

caffeic acidinhibition patternsp-hydroxycinnamic acidα-amylaseα-glucosidase

Identifiers

PMID42279759
PMCPMC13256135

What OpenQuestion holds

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LicenceCC BY
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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.