Evidence map›Paper›PMID 24603692›Full record

ArticlePloS one2014

Evaluating molecular mechanism of hypotensive peptides interactions with renin and angiotensin converting enzyme.

Rong He, Rotimi E Aluko, Xing-Rong Ju

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.1field-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

23 citing papers in PubMed, 78 citations in OpenAlex.

  1. Trial
  2. Article
  3. Review
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Frontiers in nutrition · 2022
    Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Amaranth as a Source of Antihypertensive Peptides.Frontiers in plant science · 2020
    Review
  17. Article
  18. Article
  19. 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

3 authors at 2 institutions in 2 countries.

Rong HeCollege of Food Science and Engineering, Nanjing University of Finance and Economics, Nanjing, People's Republic of China; The School of Food Science and Technology, Jiangnan University, Wuxi, People's Republic of China; Department of Human Nutritional Sciences and the Richardson Centre for Functional Foods and Nutraceuticals, University of Manitoba, Winnipeg, Manitoba, Canada.
Rotimi E AlukoDepartment of Human Nutritional Sciences and the Richardson Centre for Functional Foods and Nutraceuticals, University of Manitoba, Winnipeg, Manitoba, Canada.
Xing-Rong JuCollege of Food Science and Engineering, Nanjing University of Finance and Economics, Nanjing, People's Republic of China; The School of Food Science and Technology, Jiangnan University, Wuxi, People's Republic of China.
Jiangnan University · CNUniversity of Manitoba · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Our previous study showed that three rapeseed protein-derived peptides (TF, LY and RALP) inhibited the in vitro activities of angiotensin converting enzyme (ACE) and renin. Oral administration of these peptides to spontaneously hypertensive rats led to reductions in systolic blood pressure. In the present work, we examined the potential molecular mechanisms responsible for the ACE- and renin-inhibitory activities of these peptides. Enzyme inhibition kinetics showed competitive, non-competitive and mixed-type peptide-dependent inhibition of renin and ACE activities. Intrinsic fluorescence intensity data showed that LY and RALP have stronger binding effects on ACE molecule compared to that of TF. LY and RALP showed the highest inhibition of ACE and renin activities, respectively. Circular dichroism data showed that the inhibitory mechanism involved extensive peptide-dependent reductions in α-helix and β-sheet fractions of ACE and renin protein conformations. Molecular docking studies confirmed that the higher renin-inhibitory activity of RALP may be due to formation of several hydrogen bonds (H-bonds) with the enzyme's active site residues. The rapeseed peptides inhibited renin and ACE activities mostly through binding to enzyme active site or non-active sites and forming extensive H-bonds that distorted the normal configuration required for catalysis. Data presented from this work could enhance development of highly potent antihypertensive natural peptides or peptidomimetics.

Indexed as

Renin InhibitorsAngiotensin-Converting Enzyme InhibitorsAnimalsAntihypertensive AgentsBiocatalysisCatalytic DomainCircular DichroismKineticsMolecular Docking SimulationPeptidesPeptidyl-Dipeptidase AProtein Structure, SecondaryRats, Inbred SHRReninSpectrometry, FluorescenceAngiotensin-Converting Enzyme InhibitorsAntihypertensive AgentsPeptidesPeptidyl-Dipeptidase AReninRenin Inhibitors

Identifiers

PMID24603692
PMCPMC3946342
OpenAlexW1995200305

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.