Evidence map›Paper›PMID 28618113›Full record

ArticleMolecular nutrition & food research2017

The mechanism of interactions between tea polyphenols and porcine pancreatic alpha-amylase: Analysis by inhibition kinetics, fluorescence quenching, differential scanning calorimetry and isothermal titration calorimetry.

Lijun Sun, Michael J Gidley, Frederick J Warren

Open access · hybridAbstract read
In one paragraph

Article in Molecular nutrition & food research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
5.6field-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

18 citing papers in PubMed, 126 citations in OpenAlex.

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  7. Chemical and biochemical characterization ofFrontiers in nutrition · 2023
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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

3 authors at 2 institutions in 2 countries.

Lijun SunCentre for Nutrition and Food Sciences, ARC Centre of Excellence in Plant Cell Walls, Queensland Alliance for Agriculture and Food Innovation, The University of Queensland, Queensland, Australia.
Michael J GidleyCentre for Nutrition and Food Sciences, ARC Centre of Excellence in Plant Cell Walls, Queensland Alliance for Agriculture and Food Innovation, The University of Queensland, Queensland, Australia.
Frederick J WarrenCentre for Nutrition and Food Sciences, ARC Centre of Excellence in Plant Cell Walls, Queensland Alliance for Agriculture and Food Innovation, The University of Queensland, Queensland, Australia.
University of Queensland · AUNorwich Research Park · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

scopeThis study aims to use a combination of biochemical and biophysical methods to derive greater mechanistic understanding of the interactions between tea polyphenols and porcine pancreatic α-amylase (PPA). METHODS AND

resultsThe interaction mechanism was studied through fluorescence quenching (FQ), differential scanning calorimetry (DSC) and isothermal titration calorimetry (ITC) and compared with inhibition kinetics. The results showed that a higher quenching effect of polyphenols corresponded to a stronger inhibitory activity against PPA. The red-shift of maximum emission wavelength of PPA bound with some polyphenols indicated a potential structural unfolding of PPA. This was also suggested by the decreased thermostability of PPA with these polyphenols in DSC thermograms. Through thermodynamic binding analysis of ITC and inhibition kinetics, the equilibrium of competitive inhibition was shown to result from the binding of particularly galloylated polyphenols with specific sites on PPA. There were positive linear correlations between the reciprocal of competitive inhibition constant (1/K

conclusionThe combination of inhibition kinetics, FQ, DSC and ITC can reasonably characterize the interactions between tea polyphenols and PPA. The galloyl moiety is an important group in catechins and theaflavins in terms of binding with and inhibiting the activity of PPA.

Indexed as

AnimalsBiflavonoidsCalorimetryCalorimetry, Differential ScanningCatechinFluorescenceModels, TheoreticalPancreasPancreatic alpha-AmylasesPolyphenolsSwineTeaThermodynamicsBiflavonoidsCatechinPancreatic alpha-AmylasesPolyphenolsTeatheaflavinDifferential scanning calorimetryFluorescence quenchingInteraction mechanismIsothermal titration calorimetryTea polyphenolsα-Amylase

Identifiers

PMID28618113
PMCPMC5656823
OpenAlexW2626780962

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.