Evidence map›Paper›PMID 26543535›Full record

ArticleJournal of diabetes investigation2015

Peptide modulators of alpha-glucosidase.

Irena Roskar, Peter Molek, Miha Vodnik, Mateja Stempelj, Borut Strukelj, Mojca Lunder

Open access · goldAbstract read
In one paragraph

Article in Journal of diabetes investigation, 2015. 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
1.1field-weighted citation impact, top 23% 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, 27 citations in OpenAlex.

  1. Article
  2. An Update on Dipeptidyl Peptidase-IV Inhibiting Peptides.Current protein & peptide science · 2024
    Review
  3. UPLC-ESI-QTOF-MS Profiling of Phenolic Compounds fromMolecules (Basel, Switzerland) · 2022
    Article
  4. Article
  5. Antidiabetic bio-peptides of soft and hard wheat glutens.Food chemistry. Molecular sciences · 2022
    Article
  6. Review
  7. 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

6 authors at 1 institution in 1 country.

Irena RoskarEntrapharm d.o.o., University of Ljubljana Ljubljana, Slovenia.
Peter MolekChair of Pharmaceutical Biology, Faculty of Pharmacy, University of Ljubljana Ljubljana, Slovenia.
Miha VodnikChair of Pharmaceutical Biology, Faculty of Pharmacy, University of Ljubljana Ljubljana, Slovenia.
Mateja StempeljEntrapharm d.o.o., University of Ljubljana Ljubljana, Slovenia.
Borut StrukeljChair of Pharmaceutical Biology, Faculty of Pharmacy, University of Ljubljana Ljubljana, Slovenia.
Mojca LunderChair of Pharmaceutical Biology, Faculty of Pharmacy, University of Ljubljana Ljubljana, Slovenia.
University of Ljubljana · SI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

AIMS/

introductionAcute glucose fluctuations during the postprandial period pose great risk for cardiovascular complications and thus represent an important therapeutic approach in type 2 diabetes. In the present study, screening of peptide libraries was used to select peptides with an affinity towards mammalian intestinal alpha-glucosidase as potential leads in antidiabetic agent development. MATERIALS AND

methodsThree phage-displayed peptide libraries were used in independent selections with different elution strategies to isolate target-binding peptides. Selected peptides displayed on phage were tested to compete for an enzyme-binding site with known competitive inhibitors, acarbose and voglibose. The four best performing peptides were synthesized. Their binding to the mammalian alpha-glucosidase and their effect on enzyme activity were evaluated.

resultsTwo linear and two cyclic heptapeptides with high affinity towards intestinal alpha-glucosidase were selected. Phage-displayed as well as synthetic peptides bind into or to the vicinity of the active site on the enzyme. Both cyclic peptides inhibited enzyme activity, whereas both linear peptides increased enzyme activity.

conclusionsAlthough natural substrates of glycosidase are polysaccharides, in the present study we successfully isolated novel peptide modulators of alpha-glucosidase. Modulatory activity of selected peptides could be further optimized through peptidomimetic design. They represent promising leads for development of efficient alpha-glucosidase inhibitors.

Indexed as

Maltase glucoamylasePeptide modulatorsPhage display

Identifiers

PMID26543535
PMCPMC4627538
OpenAlexW2134401521

What OpenQuestion holds

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LicenceCC BY-NC-ND
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.