dc.creatorHerrera, Maria Georgina
dc.creatorVeuthey, Tania Vanesa
dc.creatorDodero, Veronica Isabel
dc.date.accessioned2018-08-03T20:47:24Z
dc.date.accessioned2018-11-06T11:48:21Z
dc.date.available2018-08-03T20:47:24Z
dc.date.available2018-11-06T11:48:21Z
dc.date.created2018-08-03T20:47:24Z
dc.date.issued2016-05
dc.identifierHerrera, Maria Georgina; Veuthey, Tania Vanesa; Dodero, Veronica Isabel; Self-organization of gliadin in aqueous media under physiological digestive pHs; Elsevier Science; Colloids and Surfaces B: Biointerfaces; 141; 5-2016; 565-575
dc.identifier0927-7765
dc.identifierhttp://hdl.handle.net/11336/54173
dc.identifierCONICET Digital
dc.identifierCONICET
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1859720
dc.description.abstractHere we showed that gliadin, a complex protein system related to celiac disease and other human diseases, is spontaneously self-organized in a very dilute solution at pH 3.0 and 7.0 in water under low ionic strength (10 mM NaCl). The spontaneous self-organization at pH 3.0 increases the apparent solubility due to the formation of finite sized aggregates, such as those formed in the micellization of amphiphilic molecules. Switching the pH from 3.0 to 7.0 lead to a phase separation, however part of the nano-particles are stable remaining disperse in water after centrifugation. Also, beside the pH change led to changes in protein composition and concentration, we determined that the secondary structure of both system is the same. Moreover, Tyrs are slightly more buried and Trps are slightly more exposed to water at pH 7.0 than those at pH 3.0. Electron microscopy techniques showed that both gliadin systems are composed of nanostructures and in the case of pH 7.0 amorphous microaggregates were found, too. Only nanostructures at pH 3.0 showed a micromolar binding affinity to Nile red probe, suggesting the presence of accessible hydrophobic patches which are not more accessible at pH 7.0. All our results suggest that gliadin is able to self-organized at pH 3.0 forming protein micelles type nanostructures (ζ = + 13, 42 ± 1.55 mV), meanwhile at 7.0 the decrease of superficial charge to ζ of +4, 78 ± 0.48 mV led to the formation of stable colloidal nanoparticles, unable to interact with Nile red probe. Our findings may open new perspectives for the understanding of gliadin ability to avoid proteolysis, to reach and cross the intestinal lumen and to trigger different immunological disorders.
dc.languageeng
dc.publisherElsevier Science
dc.relationinfo:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.colsurfb.2016.02.019
dc.relationinfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0927776516300984
dc.rightshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.subjectBIOPHYSICS
dc.subjectCOLLOIDS
dc.subjectELECTRON MICROSCOPY
dc.subjectGLIADIN NANOSTRUCTURES
dc.subjectGLIADIN RELATED DISORDERS
dc.subjectNILE RED BINDING
dc.titleSelf-organization of gliadin in aqueous media under physiological digestive pHs
dc.typeArtículos de revistas
dc.typeArtículos de revistas
dc.typeArtículos de revistas


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