Evidence map›Paper›PMID 31590308›Full record

ArticleBiomolecules2019

Angiotensin Converting Enzyme (ACE)-Peptide Interactions: Inhibition Kinetics, In Silico Molecular Docking and Stability Study of Three Novel Peptides Generated from Palm Kernel Cake Proteins.

Mohammad Zarei, Najib Bin Zainal Abidin, Shehu Muhammad Auwal, Shyan Yea Chay, Zaibunnisa Abdul Haiyee, Adi Md Sikin, Nazamid Saari

Open access · goldAbstract read
In one paragraph

Article in Biomolecules, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.0field-weighted citation impact, top 24% 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

10 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Screening and Molecular Mechanisms of Novel ACE-Inhibitory Peptides fromInternational journal of molecular sciences · 2022
    Article
  5. Article
  6. Review
  7. Article
  8. Article
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  10. 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 at 3 institutions in 2 countries.

Mohammad ZareiDepartment of Food Science and Technology, School of Industrial Technology, Faculty of Applied Sciences, Universiti Teknologi MARA, Shah Alam 40450, Selangor, Malaysia. mzarei.mail@gmail.com.
Najib Bin Zainal AbidinDepartment of Food Science, Faculty of Food Science and Technology, Universiti Putra Malaysia, Serdang 43400, Selangor, Malaysia.
Shehu Muhammad AuwalDepartment of Biochemistry, Faculty of Basic Medical Sciences, Bayero University, Kano 700231, Nigeria.
Shyan Yea ChayDepartment of Food Science, Faculty of Food Science and Technology, Universiti Putra Malaysia, Serdang 43400, Selangor, Malaysia.
Zaibunnisa Abdul HaiyeeDepartment of Food Science and Technology, School of Industrial Technology, Faculty of Applied Sciences, Universiti Teknologi MARA, Shah Alam 40450, Selangor, Malaysia.
Adi Md SikinDepartment of Food Science and Technology, School of Industrial Technology, Faculty of Applied Sciences, Universiti Teknologi MARA, Shah Alam 40450, Selangor, Malaysia.
Nazamid SaariDepartment of Food Science, Faculty of Food Science and Technology, Universiti Putra Malaysia, Serdang 43400, Selangor, Malaysia. nazamid@upm.edu.my.
Universiti Putra Malaysia · MYUniversiti Teknologi MARA · MYBayero University Kano · NG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Three novel peptide sequences identified from palm kernel cake (PKC) generated protein hydrolysate including YLLLK, WAFS and GVQEGAGHYALL were used for stability study against angiotensin-converting enzyme (ACE), ACE-inhibition kinetics and molecular docking studies. Results showed that the peptides were degraded at different cleavage degrees of 94%, 67% and 97% for YLLLK, WAFS and GVQEGAGHYALL, respectively, after 3 h of incubation with ACE. YLLLK was found to be the least stable (decreased ACE-inhibitory activity) compared to WAFS and GVQEGAGHYALL (increased ACE-inhibitory activity). YLLLK showed the lowest K

Indexed as

AnimalsCatalysisCatalytic DomainGene Expression RegulationHumansHydrolysisKineticsModels, MolecularMolecular Docking SimulationPalm OilPeptide FragmentsPeptidyl-Dipeptidase APlant ProteinsACE protein, humanPalm OilPeptide FragmentsPeptidyl-Dipeptidase APlant Proteinsangiotensin converting enzyme inhibitory activitykineticsmolecular dockingpeptide

Identifiers

PMID31590308
PMCPMC6843816
OpenAlexW2977954642

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.