Evidence map›Paper›PMID 36262383›Full record

ArticleFood chemistry. Molecular sciences2022

Preparation, identification, and molecular docking of novel elastase inhibitory peptide from walnut (

Yu Xiong, Peng Peng, Shi-Jia Chen, Min Chang, Qian Wang, Sheng-Nan Yin, Di-Feng Ren

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Food chemistry. Molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Food Peptides for the Nutricosmetic Industry.Antioxidants (Basel, Switzerland) · 2023
    Review
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.

Yu XiongBeijing Key Laboratory of Food Processing and Safety in Forestry, Department of Food Science and Engineering, College of Biological Sciences and Biotechnology, Beijing Forestry University, 100083 Beijing, People's Republic of China.
Peng PengBeijing Key Laboratory of Food Processing and Safety in Forestry, Department of Food Science and Engineering, College of Biological Sciences and Biotechnology, Beijing Forestry University, 100083 Beijing, People's Republic of China.
Shi-Jia ChenBeijing Key Laboratory of Food Processing and Safety in Forestry, Department of Food Science and Engineering, College of Biological Sciences and Biotechnology, Beijing Forestry University, 100083 Beijing, People's Republic of China.
Min ChangBeijing Key Laboratory of Food Processing and Safety in Forestry, Department of Food Science and Engineering, College of Biological Sciences and Biotechnology, Beijing Forestry University, 100083 Beijing, People's Republic of China.
Qian WangBeijing Key Laboratory of Food Processing and Safety in Forestry, Department of Food Science and Engineering, College of Biological Sciences and Biotechnology, Beijing Forestry University, 100083 Beijing, People's Republic of China.
Sheng-Nan YinBeijing Key Laboratory of Food Processing and Safety in Forestry, Department of Food Science and Engineering, College of Biological Sciences and Biotechnology, Beijing Forestry University, 100083 Beijing, People's Republic of China.
Di-Feng RenBeijing Key Laboratory of Food Processing and Safety in Forestry, Department of Food Science and Engineering, College of Biological Sciences and Biotechnology, Beijing Forestry University, 100083 Beijing, People's Republic of China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

This study aimed to isolate bioactive peptides with elastase inhibitory activity from walnut meal via ultrasonic enzymatic hydrolysis. The optimal hydrolysis conditions of walnut meal protein hydrolysates (WMPHs) were obtained by response surface methodology (RSM), while a molecular weight of<3 kDa fraction was analyzed by LC-MS/MS, and 556 peptides were identified. PyRx virtual screening and Autodock Vina molecular docking revealed that the pentapeptide Phe-Phe-Val-Pro-Phe (FFVPF) could interact with elastase primarily through hydrophobic interactions, hydrogen bonds, and π-sulfur bonds, with a binding energy of -5.22 kcal/mol. The verification results of inhibitory activity showed that FFVPF had better elastase inhibitory activity, with IC

Indexed as

Elastase inhibitory activityGastrointestinal digestionInhibitor based-peptideMolecular dockingWalnut meal

Identifiers

PMID36262383
PMCPMC9574760

What Socratic holds

Textmetadata
LicenceCC BY-NC-ND
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 Socratic graph.