Evidence map›Paper›PMID 33808034›Full record

ArticleNutrients2021

Trans-Epithelial Transport, Metabolism, and Biological Activity Assessment of the Multi-Target Lupin Peptide LILPKHSDAD (P5) and Its Metabolite LPKHSDAD (P5-Met).

Carmen Lammi, Gilda Aiello, Carlotta Bollati, Jianqiang Li, Martina Bartolomei, Giulia Ranaldi, Simonetta Ferruzza, Enrico Mario Alessandro Fassi, Giovanni Grazioso, Yula Sambuy and 1 more

Open access · goldAbstract read
In one paragraph

Article in Nutrients, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
7.3field-weighted citation impact, top 3% 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

13 citing papers in PubMed, 28 citations in OpenAlex.

  1. Review
  2. Review
  3. Seaweed (Journal of agricultural and food chemistry · 2025
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  5. Review
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  7. Article
  8. MOMASTAntioxidants (Basel, Switzerland) · 2023
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. 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

11 authors at 1 institution in 1 country.

Carmen LammiDepartment of Pharmaceutical Sciences, University of Milan, 20122 Milan, Italy.
Gilda AielloDepartment of Pharmaceutical Sciences, University of Milan, 20122 Milan, Italy.
Carlotta BollatiDepartment of Pharmaceutical Sciences, University of Milan, 20122 Milan, Italy.ORCID 0000-0002-5698-1325
Jianqiang LiDepartment of Pharmaceutical Sciences, University of Milan, 20122 Milan, Italy.
Martina BartolomeiDepartment of Pharmaceutical Sciences, University of Milan, 20122 Milan, Italy.ORCID 0000-0002-3851-3392
Giulia RanaldiFood and Nutrition Research Centre, CREA, 00178 Rome, Italy.
Simonetta FerruzzaFood and Nutrition Research Centre, CREA, 00178 Rome, Italy.ORCID 0000-0002-9609-9927
Enrico Mario Alessandro FassiDepartment of Pharmaceutical Sciences, University of Milan, 20122 Milan, Italy.ORCID 0000-0001-6282-4273
Giovanni GraziosoDepartment of Pharmaceutical Sciences, University of Milan, 20122 Milan, Italy.ORCID 0000-0002-3261-9356
Yula SambuyFood and Nutrition Research Centre, CREA, 00178 Rome, Italy.ORCID 0000-0003-2522-6279
Anna ArnoldiDepartment of Pharmaceutical Sciences, University of Milan, 20122 Milan, Italy.ORCID 0000-0002-0987-3014
University of Milan · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

P5 (LILPKHSDAD) is a hypocholesterolemic peptide from lupin protein with a multi-target activity, since it inhibits both 3-hydroxy-3-methylglutaryl coenzyme A reductase (HMGCoAR) and proprotein convertase subtilisin/kexin type-9 (PCSK9). This work shows that, during epithelial transport experiments, the metabolic transformation mediated by intestinal peptidases produces two main detected peptides, ILPKHSDAD (P5-frag) and LPKHSDAD (P5-met), and that both P5 and P5-met are linearly absorbed by differentiated human intestinal Caco-2 cells. Extensive comparative structural, biochemical, and cellular characterizations of P5-met and the parent peptide P5 demonstrate that both peptides have unique characteristics and share the same mechanisms of action. In fact, they exert an intrinsically multi-target behavior being able to regulate cholesterol metabolism by modulating different pathways. The results of this study also highlight the dynamic nature of bioactive peptides that may be modulated by the biological systems they get in contact with.

Indexed as

Biological TransportCaco-2 CellsHep G2 CellsHumansHydroxymethylglutaryl CoA ReductasesIntestinal MucosaLipid MetabolismLupinusPeptidesPlant ProteinsProprotein Convertase 9HMGCR protein, humanHydroxymethylglutaryl CoA ReductasesPCSK9 protein, humanPeptidesPlant ProteinsProprotein Convertase 9Caco-2 cellsfood bioactive peptidesLDLRPCSK9trans-epithelial transport

Identifiers

PMID33808034
PMCPMC8000724
OpenAlexW3134204694

What OpenQuestion holds

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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.