Self-assembly of 33-mer gliadin peptide oligomers

Herrera MG, Benedini LA, Lonez C, Schilardi PL, Hellweg T, Ruysschaert J-M, Dodero VI (2015)
Soft Matter 11(44): 8648-8660.

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Zeitschriftenaufsatz | Veröffentlicht | Englisch
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Abstract / Bemerkung
The 33-mer gliadin peptide, LQLQPF(PQPQLPY)(3)PQPQPF, is a highly immunogenic peptide involved in celiac disease and probably in other immunopathologies associated with gliadin. Herein, dynamic light scattering measurements showed that 33-mer, in the micromolar concentration range, forms polydisperse nano- and micrometer range particles in aqueous media. This behaviour is reminiscent of classical association of colloids and we hypothesized that the 33-mer peptide self-assembles into micelles that could be the precursors of 33-mer oligomers in water. Deposition of 33-mer peptide aqueous solution on bare mica generated nano- and microstructures with different morphologies as revealed by atomic force microscopy. At 6 mu M, the 33-mer is organised in isolated and clusters of spherical nanostructures. In the 60 to 250 mu M concentration range, the spherical oligomers associated mainly in linear and annular arrangements and structures adopting a "sheet'' type morphology appeared. At higher concentrations (610 mu M), mainly filaments and plaques immersed in a background of nanospherical structures were detected. The occurrence of different morphologies of oligomers and finally the filaments suggests that the unique specific geometry of the 33-mer oligomers has a crucial role in the subsequent condensation and organization of their fractal structures into the final filaments. The self-assembly process on mica is described qualitatively and quantitatively by a fractal diffusion limited aggregation (DLA) behaviour with the fractal dimension in the range of 1.62 +/- 0.02 to 1.73 +/- 0.03. Secondary structure evaluation of the oligomers by Attenuated Total Reflection FTIR spectroscopy (ATR-FTIR) revealed the existence of a conformational equilibrium of self-assembled structures, from an extended conformation to a more folded parallel beta elongated structures. Altogether, these findings provide structural and morphological information about supramolecular organization of the 33-mer peptide, which might offer new perspectives for the understanding and treatment of gliadin intolerance disorders.
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Zeitschriftentitel
Soft Matter
Band
11
Zeitschriftennummer
44
Seite
8648-8660
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Herrera MG, Benedini LA, Lonez C, et al. Self-assembly of 33-mer gliadin peptide oligomers. Soft Matter. 2015;11(44):8648-8660.
Herrera, M. G., Benedini, L. A., Lonez, C., Schilardi, P. L., Hellweg, T., Ruysschaert, J. - M., & Dodero, V. I. (2015). Self-assembly of 33-mer gliadin peptide oligomers. Soft Matter, 11(44), 8648-8660. doi:10.1039/c5sm01619c
Herrera, M. G., Benedini, L. A., Lonez, C., Schilardi, P. L., Hellweg, T., Ruysschaert, J. - M., and Dodero, V. I. (2015). Self-assembly of 33-mer gliadin peptide oligomers. Soft Matter 11, 8648-8660.
Herrera, M.G., et al., 2015. Self-assembly of 33-mer gliadin peptide oligomers. Soft Matter, 11(44), p 8648-8660.
M.G. Herrera, et al., “Self-assembly of 33-mer gliadin peptide oligomers”, Soft Matter, vol. 11, 2015, pp. 8648-8660.
Herrera, M.G., Benedini, L.A., Lonez, C., Schilardi, P.L., Hellweg, T., Ruysschaert, J.-M., Dodero, V.I.: Self-assembly of 33-mer gliadin peptide oligomers. Soft Matter. 11, 8648-8660 (2015).
Herrera, M. G., Benedini, L. A., Lonez, C., Schilardi, P. L., Hellweg, Thomas, Ruysschaert, J-M., and Dodero, V. I. “Self-assembly of 33-mer gliadin peptide oligomers”. Soft Matter 11.44 (2015): 8648-8660.

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Translational Chemistry Meets Gluten-Related Disorders.
Lammers KM, Herrera MG, Dodero VI., ChemistryOpen 7(3), 2018
PMID: 29531885

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