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Comment
. 2019 Nov 29:10:2792.
doi: 10.3389/fimmu.2019.02792. eCollection 2019.

Commentary: p31-43 Gliadin Peptide Forms Oligomers and Induces NLRP3 Inflammasome/Caspase 1- Dependent Mucosal Damage in Small Intestine

Exequiel Barrera  1 , Fernando Chirdo  2 , Sergio Pantano  1
Affiliations
Comment

Commentary: p31-43 Gliadin Peptide Forms Oligomers and Induces NLRP3 Inflammasome/Caspase 1- Dependent Mucosal Damage in Small Intestine

Exequiel Barrera et al. Front Immunol. .
No abstract available

Keywords: celiac disease; coarse grained (CG); gliadin peptides; p31-43; simulations; sirah force field.

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Figures

Figure 1
Figure 1
Structural superposition of the best matching solution between NMR derived conformations and simulation of isolated peptides (A), and peptides within the 50-mer aggregate (B). On (C), the final structures obtained by molecular dynamics of each peptide forming the oligomer (Y-axis) are compared against all the conformers reported in the NMR family of structures (X-axis). The degree of structural similarity is reported as the root mean square deviation (RMSD) between the C-alpha carbons of simulated and NMR derived conformers. Small RMSD values (red-yellow) identify high structural similarity. Simulations of P36A and F37A showed the same degree of structural similarity (not shown).
See this image and copyright information in PMC

Comment on

References

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    1. Lania G, Nanayakkara M, Maglio M, Auricchio R, Porpora M, Conte M, et al. Constitutive alterations in vesicular trafficking increase the sensitivity of cells from celiac disease patients to gliadin. Commun Biol. (2019) 2:190. 10.1038/s42003-019-0443-1 - DOI - PMC - PubMed

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