dc.creator | Herrera, Maria Georgina | |
dc.creator | Zamarreño, Fernando | |
dc.creator | Costabel, Marcelo Daniel | |
dc.creator | Ritacco, Hernán Alejandro | |
dc.creator | Hütten, Andreas | |
dc.creator | Sewald, Norbert | |
dc.creator | Dodero, Veronica Isabel | |
dc.date.accessioned | 2015-09-22T20:01:00Z | |
dc.date.accessioned | 2018-11-06T12:46:01Z | |
dc.date.available | 2015-09-22T20:01:00Z | |
dc.date.available | 2018-11-06T12:46:01Z | |
dc.date.created | 2015-09-22T20:01:00Z | |
dc.date.issued | 2014-01 | |
dc.identifier | Herrera, Maria Georgina; Zamarreño, Fernando; Costabel, Marcelo Daniel; Ritacco, Hernán Alejandro; Hütten, Andreas; et al.; Circular Dichroism and Electron Microscopy Studies In Vitro of 33-mer Gliadin Peptide Revealed Secondary Structure Transition and Supramolecular Organization; Wiley; Biopolymers; 101; 1; 1-2014; 96-106 | |
dc.identifier | 1097-0282 | |
dc.identifier | http://hdl.handle.net/11336/2046 | |
dc.identifier.uri | http://repositorioslatinoamericanos.uchile.cl/handle/2250/1869899 | |
dc.description.abstract | Gliadin, a protein present in wheat, rye, and barley, undergoes incomplete enzymatic degradation during digestion, producing an immunogenic 33-mer peptide, LQLQPF(PQPQLPY)3 PQPQPF. The special features of 33-mer that provoke a break in its tolerance leading to gliadin sensitivity and celiac disease remains elusive. Herein, it is reported that 33-mer gliadin peptide was not only able to fold into polyproline II secondary structure but also depending on concentration resulted in conformational transition and self-assembly under aqueous condition, pH 7.0. A 33-mer dimer is presented as one initial possible step in the self-assembling process obtained by partial electrostatics charge distribution calculation and molecular dynamics. In addition, electron microscopy experiments revealed supramolecular organization of 33-mer into colloidal nanospheres. In the presence of 1 mMsodium citrate, 1 mMsodium borate, 1 mMsodium phosphate buffer, 15 mMNaCl, the nanospheres were stabilized, whereas in water, a linear organization and formation of fibrils were observed. It is hypothesized that the self-assembling process could be the result of the combination of hydrophobic effect, intramolecular hydrogen bonding, and electrostatic complementarity due to 33-mer’s high content of proline and glutamine amino acids and its calculated nonionic amphiphilic character. Although, performed in vitro, these experiments have revealed new features of the 33-mer gliadin peptide that could represent an important and unprecedented event in the early stage of 33-mer interaction with the gut mucosa prior to onset of inflammation. Moreover, these findings may open new perspectives for the understanding and treatment of gliadin intolerance disorders. | |
dc.language | eng | |
dc.publisher | Wiley | |
dc.relation | info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1002/bip.22288 | |
dc.relation | info:eu-repo/semantics/altIdentifier/url/http://onlinelibrary.wiley.com/doi/10.1002/bip.22288/abstract | |
dc.rights | https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ | |
dc.rights | info:eu-repo/semantics/restrictedAccess | |
dc.subject | 33-MER | |
dc.subject | GLIADIN PEPTIDE | |
dc.subject | CIRCULAR-DICHROISM | |
dc.subject | ELECTRON MICROSCOPY | |
dc.subject | SUPRAMOLECULAR ORGANIZATION | |
dc.subject | GLIADIN INTOLERANCE | |
dc.title | Circular Dichroism and Electron Microscopy Studies In Vitro of 33-mer Gliadin Peptide Revealed Secondary Structure Transition and Supramolecular Organization | |
dc.type | Artículos de revistas | |
dc.type | Artículos de revistas | |
dc.type | Artículos de revistas | |