Evidence map›Paper›PMID 38137191›Full record

ArticleFoods (Basel, Switzerland)2023

Virtual Screening Technology for Two Novel Peptides in Soybean as Inhibitors of α-Amylase and α-Glucosidase.

Xiyao Tang, Xu Chen, Hong Wang, Jinyi Yang, Lin Li, Jie Zhu, Yujia Liu

Open access · goldAbstract read
In one paragraph

Article in Foods (Basel, Switzerland), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
2.0field-weighted citation impact, top 13% of its field
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

6 citing papers in PubMed, 13 citations in OpenAlex.

  1. Physicochemical, Technofunctional and Antiglycaemic Properties ofInternational journal of food science · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Construction of PCR-SERS Method for Detection ofFoods (Basel, Switzerland) · 2024
    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

7 authors at 2 institutions in 1 country.

Xiyao TangKey Laboratory of Healthy Food Development and Nutrition Regulation of China National Light Industry, School of Life and Health Technology, Dongguan University of Technology, Dongguan 523808, China.
Xu ChenKey Laboratory of Healthy Food Development and Nutrition Regulation of China National Light Industry, School of Life and Health Technology, Dongguan University of Technology, Dongguan 523808, China.
Hong WangCollege of Food Science, South China Agricultural University, Guangzhou 510642, China.
Jinyi YangCollege of Food Science, South China Agricultural University, Guangzhou 510642, China.ORCID 0000-0002-6457-3719
Lin LiKey Laboratory of Healthy Food Development and Nutrition Regulation of China National Light Industry, School of Life and Health Technology, Dongguan University of Technology, Dongguan 523808, China.
Jie ZhuKey Laboratory of Healthy Food Development and Nutrition Regulation of China National Light Industry, School of Life and Health Technology, Dongguan University of Technology, Dongguan 523808, China.ORCID 0000-0002-9107-9628
Yujia LiuKey Laboratory of Healthy Food Development and Nutrition Regulation of China National Light Industry, School of Life and Health Technology, Dongguan University of Technology, Dongguan 523808, China.
Dongguan University of Technology · CNSouth China Agricultural University · CN

Funding

National Natural Science Foundation of China 31901682National Natural Science Foundation of China 32202010
6 · The paper itself

Abstract

Soybean peptides (SPs) have bioactivities of enzyme inhibition that are beneficial to human health, but their mechanism is not clear. This study aimed to identify peptide fragments in SPs that simultaneously inhibit α-amylase and α-glucosidase and to explore their enzyme inhibition mechanism. Firstly, the inhibitory activity of SPs against the enzymes was determined. And two octapeptides, LDQTPRVF and SRNPIYSN, were identified for the first time by using HPLC-QTOF-MS/MS and virtual screening. Molecular simulation results showed that hydrogen bonds and π-π bonds were the key factors, and the N-terminal (Leu and Ser) and C-terminal (Phe) of peptide were important inhibiting sites. Both octapeptides were synthesized, and their IC50 values were 3.08 and 5.58 mmol/L for α-amylase, and 2.52 and 4.57 mmol/L for α-glucosidase, respectively. This study provided evidence for SPs as a potential inhibitor of α-amylase and α-glucosidase in special dietary foods.

Indexed as

inhibition activitymolecular dockingsoybean peptidesα-amylaseα-glucosidase

Identifiers

PMID38137191
PMCPMC10743026
OpenAlexW4389388935

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.