Evidence map›Paper›PMID 36161684›Full record

ArticleChembiochem : a European journal of chemical biology2022

Thin-Plate Superstructures of the Immunogenic 33-mer Gliadin Peptide.

Maria Georgina Herrera, Maria Julia Amundarain, Franscesco Nicoletti, Marcus Drechsler, Marcelo Costabel, Pier Luigi Gentili, Veronica Isabel Dodero

Open access · hybridAbstract read
In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
1.0field-weighted citation impact, top 25% 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

3 citing papers in PubMed, 6 citations in OpenAlex.

  1. Review
  2. Article
  3. Thin-Plate Superstructures of the Immunogenic 33-mer Gliadin Peptide.Chembiochem : a European journal of chemical biology · 2022
    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

7 authors at 4 institutions in 3 countries.

Maria Georgina HerreraFaculty of Chemistry, OCIII, Bielefeld University, Universitätsstr. 25, 33615, Bielefeld, Germany.
Maria Julia AmundarainInstituto de Física del Sur (IFISUR), Departamento de Física, Universidad Nacional del Sur (UNS), CONICET Av. L. N. Alem, 1253, B8000CPB -, Bahía Blanca, Argentina.
Franscesco NicolettiFaculty of Chemistry, OCIII, Bielefeld University, Universitätsstr. 25, 33615, Bielefeld, Germany.
Marcus DrechslerBavarian Polymer Institute, University Bayreuth, Universitaetsstr. 30, 95447, Bayreuth, Germany.ORCID 0000-0001-7192-7821
Marcelo CostabelInstituto de Física del Sur (IFISUR), Departamento de Física, Universidad Nacional del Sur (UNS), CONICET Av. L. N. Alem, 1253, B8000CPB -, Bahía Blanca, Argentina.
Pier Luigi GentiliDepartment of Chemistry, Biology, and Biotechnology, Università degli Studi di Perugia, Via Elce di Sotto 8, 06123, Perugia, Italy.
Veronica Isabel DoderoFaculty of Chemistry, OCIII, Bielefeld University, Universitätsstr. 25, 33615, Bielefeld, Germany.ORCID 0000-0001-7937-1880
Bielefeld University · DEConsejo Nacional de Investigaciones Científicas y Técnicas · ARBavarian Polymer Institute · DEUniversity of Perugia · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Gluten related-disorders have a prevalence of 1-5 % worldwide triggered by the ingestion of gluten proteins in wheat, rye, barley, and some oats. In wheat gluten, the most studied protein is gliadin, whose immunodominant 33-mer amino acid fragment remains after digestive proteolysis and accumulates in the gut mucosa. Here, we report the formation of 33-mer thin-plate superstructures using intrinsic tyrosine (Tyr) steady-state fluorescence anisotropy and cryo-TEM in combination with water tension measurements. Furthermore, we showed that fluorescence decay measurements of 33-mer intrinsic fluorophore Tyr provided information on the early stages of the formation of the thin-plate structures. Finally, conformational analysis of Tyr residues using minimalist models by molecular dynamic simulations (MD) demonstrated that changes in Tyr rotamer states depend on the oligomerization stage. Our findings further advance the understanding of the formation of the 33-mer gliadin peptide superstructures and their relation to health and disease.

Indexed as

GliadinGlutensPeptide FragmentsPeptidesProteinsTriticumGliadinGlutensPeptide FragmentsPeptidesProteins33-mer gliadin peptidesPPII secondary structureself-assemblysupramolecular chemistrythin-plate structures

Identifiers

PMID36161684
PMCPMC9828358
OpenAlexW4297239013

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.