Evidence map›Paper›PMID 31145747›Full record

ArticlePloS one2019

Identification, structure-activity relationship and in silico molecular docking analyses of five novel angiotensin I-converting enzyme (ACE)-inhibitory peptides from stone fish (Actinopyga lecanora) hydrolysates.

Shehu Muhammad Auwal, Najib Zainal Abidin, Mohammad Zarei, Chin Ping Tan, Nazamid Saari

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
3.2field-weighted citation impact, top 7% 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

29 citing papers in PubMed, 81 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Phytotherapeutic potential ofIn silico pharmacology · 2024
    Article
  13. Article
  14. Review
  15. Production, identification,Frontiers in nutrition · 2023
    Article
  16. Article
  17. Research on ACEI of Low-Molecular-Weight Peptides fromMolecules (Basel, Switzerland) · 2022
    Article
  18. Review
  19. Conventional andFood chemistry: X · 2022
    Article
  20. 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

5 authors at 2 institutions in 2 countries.

Shehu Muhammad AuwalDepartment of Food Science, Faculty of Food Science and Technology, Universiti Putra Malaysia, Serdang, Selangor, Malaysia.
Najib Zainal AbidinDepartment of Food Science, Faculty of Food Science and Technology, Universiti Putra Malaysia, Serdang, Selangor, Malaysia.
Mohammad ZareiDepartment of Food Science and Technology, School of Industrial Technology, Faculty of Applied Sciences, Universiti Teknologi MARA, Shah Alam, Selangor, Malaysia.ORCID 0000-0003-1573-347X
Chin Ping TanDepartment of Food Technology, Faculty of Food Science and Technology, Universiti Putra Malaysia, Serdang, Selangor, Malaysia.
Nazamid SaariDepartment of Food Science, Faculty of Food Science and Technology, Universiti Putra Malaysia, Serdang, Selangor, Malaysia.ORCID 0000-0002-4185-9415
Universiti Putra Malaysia · MYUniversiti Teknologi MARA · MY

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Stone fish is an under-utilized sea cucumber with many health benefits. Hydrolysates with strong ACE-inhibitory effects were generated from stone fish protein under the optimum conditions of hydrolysis using bromelain and fractionated based on hydrophobicity and isoelectric properties of the constituent peptides. Five novel peptide sequences with molecular weight (mw) < 1000 daltons (Da) were identified using LC-MS/MS. The peptides including Ala-Leu-Gly-Pro-Gln-Phe-Tyr (794.44 Da), Lys-Val-Pro-Pro-Lys-Ala (638.88 Da), Leu-Ala-Pro-Pro-Thr-Met (628.85 Da), Glu-Val-Leu-Ile-Gln (600.77 Da) and Glu-His-Pro-Val-Leu (593.74 Da) were evaluated for ACE-inhibitory activity and showed IC50 values of 0.012 mM, 0.980 mM, 1.310 mM, 1.440 mM and 1.680 mM, respectively. The ACE-inhibitory effects of the peptides were further verified using molecular docking study. The docking results demonstrated that the peptides exhibit their effect mainly via hydrogen and electrostatic bond interactions with ACE. These findings provide evidence about stone fish as a valuable source of raw materials for the manufacture of antihypertensive peptides that can be incorporated to enhance therapeutic relevance and commercial significance of formulated functional foods.

Indexed as

FishesMolecular Docking SimulationMolecular Dynamics SimulationAmino Acid SequenceAngiotensin-Converting Enzyme InhibitorsAnimalsChromatography, LiquidHydrophobic and Hydrophilic InteractionsMolecular StructurePeptidesProtein ConformationProtein HydrolysatesStructure-Activity RelationshipTandem Mass SpectrometryAngiotensin-Converting Enzyme InhibitorsPeptidesProtein Hydrolysates

Identifiers

PMID31145747
PMCPMC6542528
OpenAlexW2951021924

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.