Structural conformation and self-assembly process of p31-43 gliadin peptide in aqueous solution. Implications for celiac disease.

Herrera MG, Gomez Castro MF, Prieto E, Barrera E, Dodero VI, Pantano S, Chirdo F (2019)
The FEBS journal: febs.15109.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
 
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Autor*in
Herrera, Maria Georgina; Gomez Castro, Maria Florencia; Prieto, Eduardo; Barrera, Exequiel; Dodero, Veronica IsabelUniBi ; Pantano, Sergio; Chirdo, Fernando
Abstract / Bemerkung
Celiac Disease (CeD) is a highly prevalent chronic immune-mediated enteropathy developed in genetically predisposed individuals after ingestion of a group of wheat proteins (called gliadins and glutenins). The 13mer alpha-gliadin peptide, p31-43, induces proinflammatory responses, observed by in vitro assays and animal models, that may contribute to innate immune mechanisms of CeD pathogenesis. Since a cellular receptor for p31-43 has not been identified, this raises the question of whether this peptide could mediate different biological effects. In this work, we aimed to characterize the p31-43 secondary structure by different biophysical and in silico techniques. By Dynamic Light Scattering (DLS) and using an oligomer/fibril-sensitive fluorescent probe, we showed the presence of oligomers of this peptide in solution. Furthermore, Atomic Force Microscopy (AFM) analysis showed p31-43 oligomers with different height distribution. Also, peptide concentration had a very strong influence on peptide self-organization process. Oligomers gradually increased their size at lower concentration. Whereas, at higher ones, oligomers increased their complexity, forming branched structures. By Circular Dichroism, we observed that p31-43 self-organized in a poly-proline II conformation in equilibrium with beta-sheets-like structures, whose pH remained stable in the range of 3 to 8. In addition, these findings were supported by Molecular Dynamics Simulation. The formation of p31-43 nanostructures with increased beta-sheet structure may help to explain the molecular etiopathogenesis in the induction of pro-inflammatory effects and subsequent damage at the intestinal mucosa in CeD. © 2019 Federation of European Biochemical Societies.
Erscheinungsjahr
2019
Zeitschriftentitel
The FEBS journal
Art.-Nr.
febs.15109
ISSN
1742-464x
eISSN
1742-4658
Page URI
https://pub.uni-bielefeld.de/record/2938557

Zitieren

Herrera MG, Gomez Castro MF, Prieto E, et al. Structural conformation and self-assembly process of p31-43 gliadin peptide in aqueous solution. Implications for celiac disease. The FEBS journal. 2019: febs.15109.
Herrera, M. G., Gomez Castro, M. F., Prieto, E., Barrera, E., Dodero, V. I., Pantano, S., & Chirdo, F. (2019). Structural conformation and self-assembly process of p31-43 gliadin peptide in aqueous solution. Implications for celiac disease. The FEBS journal, febs.15109. doi:10.1111/febs.15109
Herrera, M. G., Gomez Castro, M. F., Prieto, E., Barrera, E., Dodero, V. I., Pantano, S., and Chirdo, F. (2019). Structural conformation and self-assembly process of p31-43 gliadin peptide in aqueous solution. Implications for celiac disease. The FEBS journal:febs.15109.
Herrera, M.G., et al., 2019. Structural conformation and self-assembly process of p31-43 gliadin peptide in aqueous solution. Implications for celiac disease. The FEBS journal, : febs.15109.
M.G. Herrera, et al., “Structural conformation and self-assembly process of p31-43 gliadin peptide in aqueous solution. Implications for celiac disease.”, The FEBS journal, 2019, : febs.15109.
Herrera, M.G., Gomez Castro, M.F., Prieto, E., Barrera, E., Dodero, V.I., Pantano, S., Chirdo, F.: Structural conformation and self-assembly process of p31-43 gliadin peptide in aqueous solution. Implications for celiac disease. The FEBS journal. : febs.15109 (2019).
Herrera, Maria Georgina, Gomez Castro, Maria Florencia, Prieto, Eduardo, Barrera, Exequiel, Dodero, Veronica Isabel, Pantano, Sergio, and Chirdo, Fernando. “Structural conformation and self-assembly process of p31-43 gliadin peptide in aqueous solution. Implications for celiac disease.”. The FEBS journal (2019): febs.15109.

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