Evidence map›Paper›PMID 27043546›Full record

ArticleInternational journal of molecular sciences2016

Gastrointestinal Endogenous Protein-Derived Bioactive Peptides: An in Vitro Study of Their Gut Modulatory Potential.

Lakshmi A Dave, Maria Hayes, Leticia Mora, Carlos A Montoya, Paul J Moughan, Shane M Rutherfurd

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.4field-weighted citation impact, top 18% 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

7 citing papers in PubMed, 23 citations in OpenAlex.

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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

6 authors at 4 institutions in 3 countries.

Lakshmi A DaveThe Riddet Institute, Massey University, Private Bag 11222, Palmerston North 4442, New Zealand. Lakshdavewn@gmail.com.
Maria HayesTeagasc, The Irish Agricultural and Food Development Authority, Food BioSciences Department, Ashtown, Dublin 15, Ireland. Maria.Hayes@teagasc.ie.
Leticia MoraInstituto de Agroquı́mica y Tecnologı́a de Alimentos (CSIC), Avenida Agustín Escardino 7, 46980 Paterna, Valencia 46002, Spain. lemoso@iata.csic.es.
Carlos A MontoyaThe Riddet Institute, Massey University, Private Bag 11222, Palmerston North 4442, New Zealand. Carlos.Montoya@massey.ac.nz.
Paul J MoughanThe Riddet Institute, Massey University, Private Bag 11222, Palmerston North 4442, New Zealand. P.MMoughan@massey.ac.nz.
Shane M RutherfurdThe Riddet Institute, Massey University, Private Bag 11222, Palmerston North 4442, New Zealand. S.M.Rutherfurd@massey.ac.nz.
Massey University · NZTeagasc - The Irish Agriculture and Food Development Authority · IEInstituto de Agroquímica y Tecnología de Alimentos · ESRiddet Institute · NZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A recently proposed paradigm suggests that, like their dietary counterparts, digestion of gastrointestinal endogenous proteins (GEP) may also produce bioactive peptides. With an aim to test this hypothesis, in vitro digests of four GEP namely; trypsin (TRYP), lysozyme (LYS), mucin (MUC), serum albumin (SA) and a dietary protein chicken albumin (CA) were screened for their angiotensin-I converting (ACE-I), renin, platelet-activating factor-acetylhydrolase (PAF-AH) and dipeptidyl peptidase-IV inhibitory (DPP-IV) and antioxidant potential following simulated in vitro gastrointestinal digestion. Further, the resultant small intestinal digests were enriched to obtain peptides between 3-10 kDa in size. All in vitro digests of the four GEP were found to inhibit ACE-I compared to the positive control captopril when assayed at a concentration of 1 mg/mL, while the LYS < 3-kDa permeate fraction inhibited renin by 40% (±1.79%). The LYS < 10-kDa fraction inhibited PAF-AH by 39% (±4.34%), and the SA < 3-kDa fraction inhibited DPP-IV by 45% (±1.24%). The MUC < 3-kDa fraction had an ABTS-inhibition antioxidant activity of 150 (±24.79) µM trolox equivalent and the LYS < 10-kDa fraction inhibited 2,2-Diphenyl-1-picrylhydrazyl (DPPH) by 54% (±1.62%). Moreover, over 190 peptide-sequences were identified from the bioactive GEP fractions. The findings of the present study indicate that GEP are a significant source of bioactive peptides which may influence gut function.

Indexed as

1-Alkyl-2-acetylglycerophosphocholine EsteraseAlbuminsAmino Acid SequenceAnimalsAntioxidantsBiphenyl CompoundsChickensDipeptidyl Peptidase 4HumansIntestinal MucosaMucinsMuramidasePeptidesPeptidyl-Dipeptidase APicratesRenin1,1-diphenyl-2-picrylhydrazyl1-Alkyl-2-acetylglycerophosphocholine EsteraseAlbuminsAntioxidantsBiphenyl CompoundsDipeptidyl Peptidase 4MucinsMuramidasePeptidesPeptidyl-Dipeptidase APicratesPLA2G7 protein, humanReninRenin Inhibitorsangiotensin-I converting enzyme (ACE-I) inhibitionantioxidant peptidesdipeptidyl peptidase IV inhibitiongut non-dietary proteinslysozymerenin inhibitionserum albumin

Identifiers

PMID27043546
PMCPMC4848938
OpenAlexW2316144885

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.