Evidence map›Paper›PMID 36359988›Full record

ArticleFoods (Basel, Switzerland)2022

In-Silico Analysis and Antidiabetic Effect of α-Amylase and α-Glucosidase Inhibitory Peptides from Lupin Protein Hydrolysate: Enzyme-Peptide Interaction Study Using Molecular Docking Approach.

Gbemisola J Fadimu, Asgar Farahnaky, Harsharn Gill, Olusegun A Olalere, Chee-Yuen Gan, Tuyen Truong

Open access · goldAbstract read
In one paragraph

Article in Foods (Basel, Switzerland), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
3.3field-weighted citation impact, top 6% 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

16 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Metabolite profiling and molecular dynamics-basedFrontiers in plant science · 2026
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Anti-obesity peptides from food: Production, evaluation, sources, and commercialization.Comprehensive reviews in food science and food safety · 2025
    Review
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
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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

6 authors at 3 institutions in 3 countries.

Gbemisola J FadimuSchool of Science, RMIT University, GPO Box 2476, Melbourne, VIC 3001, Australia.ORCID 0000-0003-4736-5106
Asgar FarahnakySchool of Science, RMIT University, GPO Box 2476, Melbourne, VIC 3001, Australia.
Harsharn GillSchool of Science, RMIT University, GPO Box 2476, Melbourne, VIC 3001, Australia.
Olusegun A OlalereAnalytical Biochemistry Research Center (ABrC), Universiti Sains Malaysia, University Innovation Incubator Building, SAINS@USM Campus, Bayan Baru 11900, Penang, Malaysia.ORCID 0000-0002-4382-7281
Chee-Yuen GanAnalytical Biochemistry Research Center (ABrC), Universiti Sains Malaysia, University Innovation Incubator Building, SAINS@USM Campus, Bayan Baru 11900, Penang, Malaysia.ORCID 0000-0002-6509-1068
Tuyen TruongSchool of Science, RMIT University, GPO Box 2476, Melbourne, VIC 3001, Australia.
RMIT University · AUUniversiti Sains Malaysia · MYRMIT Vietnam · VN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The use of natural ingredients for managing diabetes is becoming more popular in recent times due to the several adverse effects associated with synthetic antidiabetic medications. In this study, we investigated the in vitro antidiabetic potential (through inhibition of α-glucosidase (AG) and α-amylase (AA)) of hydrolysates from lupin proteins pretreated with ultrasound and hydrolyzed using alcalase (ACT) and flavourzyme (FCT). We further fractionated ACT and FCT into three molecular weight fractions. Unfractionated ACT and FCT showed significantly (p < 0.05) higher AG (IC50 value = 1.65 mg/mL and 1.91 mg/mL) and AA (IC50 value = 1.66 mg/mL and 1.98 mg/mL) inhibitory activities than their ultrafiltrated fractions, where lower IC50 values indicate higher inhibitory activities. Then, ACT and FCT were subjected to peptide sequencing using LC-MS-QTOF to identify the potential AG and AA inhibitors. Molecular docking was performed on peptides with the highest number of hotspots and PeptideRanker score to study their interactions with AG and AA enzymes. Among the peptides identified, SPRRF, FE, and RR were predicted to be the most active peptides against AG, while AA inhibitors were predicted to be RPR, PPGIP, and LRP. Overall, hydrolysates prepared from lupin proteins using alcalase and flavourzyme may be useful in formulating functional food for managing diabetics.

Indexed as

bioactive peptideLC-MS QTOFlupin protein hydrolysateα-amylaseα-glucosidase

Identifiers

PMID36359988
PMCPMC9656729
OpenAlexW4307635388

What OpenQuestion holds

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LicenceCC BY
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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.