Evidence map›Paper›PMID 34681729›Full record

ArticleInternational journal of molecular sciences2021

IAF, QGF, and QDF Peptides Exhibit Cholesterol-Lowering Activity through a Statin-like HMG-CoA Reductase Regulation Mechanism: In Silico and In Vitro Approach.

Mariana Silva, Biane Philadelpho, Johnnie Santos, Victória Souza, Caio Souza, Victória Santiago, Jaff Silva, Carolina Souza, Francine Azeredo, Marcelo Castilho and 2 more

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
2.6field-weighted citation impact, top 9% 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

5 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Special Issue "Peptides for Health Benefits 2021".International journal of molecular sciences · 2024
    Article
  5. 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

12 authors at 2 institutions in 1 country.

Mariana SilvaSchool of Pharmacy, Federal University of Bahia, Salvador 40170-115, BA, Brazil.
Biane PhiladelphoSchool of Pharmacy, Federal University of Bahia, Salvador 40170-115, BA, Brazil.
Johnnie SantosSchool of Pharmacy, Federal University of Bahia, Salvador 40170-115, BA, Brazil.ORCID 0000-0002-3692-6388
Victória SouzaSchool of Pharmacy, Federal University of Bahia, Salvador 40170-115, BA, Brazil.
Caio SouzaSchool of Pharmacy, Federal University of Bahia, Salvador 40170-115, BA, Brazil.
Victória SantiagoSchool of Pharmacy, Federal University of Bahia, Salvador 40170-115, BA, Brazil.
Jaff SilvaSchool of Pharmacy, Federal University of Bahia, Salvador 40170-115, BA, Brazil.ORCID 0000-0002-0455-6458
Carolina SouzaSchool of Pharmacy, Federal University of Bahia, Salvador 40170-115, BA, Brazil.
Francine AzeredoSchool of Pharmacy, Federal University of Bahia, Salvador 40170-115, BA, Brazil.
Marcelo CastilhoSchool of Pharmacy, Federal University of Bahia, Salvador 40170-115, BA, Brazil.ORCID 0000-0002-9563-5679
Eduardo CilliChemistry Institute, Sao Paulo State University, Araraquara 14800-900, SP, Brazil.ORCID 0000-0002-4767-0904
Ederlan FerreiraSchool of Pharmacy, Federal University of Bahia, Salvador 40170-115, BA, Brazil.ORCID 0000-0003-3558-7019
Universidade Federal da Bahia · BRUniversidade Estadual Paulista (Unesp) · BR

Funding

National Council for Scientific and Technological Development CNPq, nº 426235/2016-9São Paulo Research Foundation (FAPESP, nº 13/07600-3, and nº 14/50926-0
6 · The paper itself

Abstract

In this study, in silico approaches are employed to investigate the binding mechanism of peptides derived from cowpea β-vignin and HMG-CoA reductase. With the obtained information, we designed synthetic peptides to evaluate their in vitro enzyme inhibitory activity. In vitro, the total protein extract and <3 kDa fraction, at 5000 µg, support this hypothesis (95% and 90% inhibition of HMG-CoA reductase, respectively). Ile-Ala-Phe, Gln-Gly-Phe, and Gln-Asp-Phe peptides were predicted to bind to the substrate binding site of HMGCR via HMG-CoAR. In silico, it was established that the mechanism of HMG-CoA reductase inhibition largely entailed mimicking the interactions of the decalin ring of simvastatin and via H-bonding; in vitro studies corroborated the predictions, whereby the HMG-CoA reductase activity was decreased by 69%, 77%, and 78%, respectively. Our results suggest that Ile-Ala-Phe, Gln-Gly-Phe, and Gln-Asp-Phe peptides derived from cowpea β-vignin have the potential to lower cholesterol synthesis through a statin-like regulation mechanism.

Indexed as

Amino Acid SequenceAnimalsBinding SitesCatalytic DomainHalf-LifeHydrogen BondingHydroxymethylglutaryl-CoA Reductase InhibitorsHydroxymethylglutaryl CoA ReductasesMolecular Docking SimulationPeptidesPlant ProteinsSimvastatinVignaHydroxymethylglutaryl-CoA Reductase InhibitorsHydroxymethylglutaryl CoA ReductasesPeptidesPlant ProteinsSimvastatincompetitive HMG-CoA reductase inhibitorcowpea peptidesmolecular dockingpharmacokinetic properties

Identifiers

PMID34681729
PMCPMC8538380
OpenAlexW3207699078

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.