Self-organization of gliadin in aqueous media under physiological digestive pHs

Herrera, María Georgina; Veuthey, Tania; Dodero, Verónica Isabel

doi:10.1016/j.colsurfb.2016.02.019

Cited by 29 publications

(27 citation statements)

References 70 publications

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“…Gliadin nanoparticles formation was reported in distilled water (probably at pH 6–7) [33]. Then, self-organization capabilities of 33-mer peptide were investigated under gastrointestinal environment [34]. The spontaneous self-organization at pH 3.0 leads to the formation of aggregates such as micelles of amphiphilic molecules.…”

Section: Classification and Structure Of Gluten Proteinsmentioning

confidence: 99%

Properties of Gluten Intolerance: Gluten Structure, Evolution, Pathogenicity and Detoxification Capabilities

2016

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Theterm gluten intolerance may refer to three types of human disorders: autoimmune celiac disease (CD), allergy to wheat and non-celiac gluten sensitivity (NCGS). Gluten is a mixture of prolamin proteins present mostly in wheat, but also in barley, rye and oat. Gluten can be subdivided into three major groups: S-rich, S-poor and high molecular weight proteins. Prolamins within the groups possess similar structures and properties. All gluten proteins are evolutionarily connected and share the same ancestral origin. Gluten proteins are highly resistant to hydrolysis mediated by proteases of the human gastrointestinal tract. It results in emergence of pathogenic peptides, which cause CD and allergy in genetically predisposed people. There is a hierarchy of peptide toxicity and peptide recognition by T cells. Nowadays, there are several ways to detoxify gluten peptides: the most common is gluten-free diet (GFD), which has proved its effectiveness; prevention programs, enzymatic therapy, correction of gluten pathogenicity pathways and genetically modified grains with reduced immunotoxicity. A deep understanding of gluten intolerance underlying mechanisms and detailed knowledge of gluten properties may lead to the emergence of novel effective approaches for treatment of gluten-related disorders.

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Section: Classification and Structure Of Gluten Proteinsmentioning

confidence: 99%

Properties of Gluten Intolerance: Gluten Structure, Evolution, Pathogenicity and Detoxification Capabilities

2016

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“…In the case of commercial gliadin, the buffering effect occurs at pH 3.0 when it is dissolved in 0.001 M HCl. Also, mainly the alpha isoform remains in the aqueous phase [8]. Under dilute concentration, gliadin is self-organised forming micelle-type aggregates as characterised by spectroscopic methods and conventional electron microscopy [8].…”

Section: Accepted Manuscript Introductionmentioning

confidence: 99%

“…Also, mainly the alpha isoform remains in the aqueous phase [8]. Under dilute concentration, gliadin is self-organised forming micelle-type aggregates as characterised by spectroscopic methods and conventional electron microscopy [8]. This study aims to get a better insight into gliadin supramolecular organisation in dilute aqueous solution at pH 3.0 and 10 mM NaCl using dynamic light scattering (DLS), cryogenic transmission electron microscopy (cryo-TEM) and small angle X-ray scattering (SAXS) experiments.…”

Section: Accepted Manuscript Introductionmentioning

confidence: 99%

Insights into gliadin supramolecular organization at digestive pH 3.0

Herrera

Vazquez

Sreij

et al. 2018

Colloids and Surfaces B: Biointerfaces

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Alpha-gliadin is a highly immunogenic protein from wheat, which is associated with many human diseases, like celiac disease and non-celiac gluten sensitivity. Because of that, gliadin solution is subject to intense biomedical research. However, the physicochemical nature of the employed gliadin solution at physiological pH is not understood. Herein, we present a supramolecular evaluation of the alpha-gliadin protein in water at pH 3.0 by dynamic light scattering (DLS), cryo-transmission electron microscopy (cryo-TEM) and small-angle-.X-ray scattering (SAXS). We report that at 0.5 wt% concentration (0.1 mg/ml), gliadin is already a colloidal polydisperse system with an average hydrodynamic radius of 30 ± 10 nm. By cryo-TEM, we detected mainly large clusters. However, it was possible to visualise for the first time prolate oligomers of around 68 nm and 103 nm, minor and major axis, respectively. SAXS experiments support the existence of prolate/rod-like structures. At 1.5 wt% concentration gliadin dimers, small oligomers and large clusters coexist. The radius of gyration (R) of gliadin dimer is 5.72 ± 0.23 nm with a dimer cross-section (R) of 1.63 nm, and an average length of around 19 nm, this suggests that gliadin dimers are formed longitudinally. Finally, our alpha-gliadin 3D model, obtained by ab initio prediction and analysed by molecular dynamics (MD), predicts that two surfaces prone to aggregation are exposed to the solvent, at the C-terminus. We hypothesise that this region may be involved in the dimerisation process of alpha-gliadin.

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“…This behavior is indicative of NR binding to gliadin and suggests that hydrophobic sites are accessible at pH 3.0. These results further indicate that at pH 3.0 the system is self‐organized as micellar nanostructures, whereas at pH 7.0 the structures have a lower surface charge (from +13 mV at pH 3.0 to +4 mV at pH 7.0) and colloidal nano‐ and microparticles are detected …”

Section: The Self‐assembly Properties Of Gliadin: a Supramolecular Viewmentioning

confidence: 67%

“… Supramolecular organization of gliadin in aqueous medium reported by Herrera et al . Although both solutions are clear and transparent, gliadin molecules are not randomly dispersed in water; instead, they self‐assemble to form micellar oligomers or nanoparticles depending on the pH value.…”

Section: The Self‐assembly Properties Of Gliadin: a Supramolecular Viewmentioning

confidence: 91%

Translational Chemistry Meets Gluten‐Related Disorders

2018

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Gluten‐related disorders are a complex group of diseases that involve the activation of the immune system triggered by the ingestion of gluten. Among these, celiac disease, with a prevalence of 1 %, is the most investigated, but recently, a new pathology, named nonceliac gluten sensitivity, was reported with a general prevalence of 7 %. Finally, there other less‐prevalent gluten‐related diseases such as wheat allergy, gluten ataxia, and dermatitis herpetiformis (with an overall prevalence of less than 0.1 %). As mentioned, the common molecular trigger is gluten, a complex mixture of storage proteins present in wheat, barley, and a variety of oats that are not fully degraded by humans. The most‐studied protein related to disease is gliadin, present in wheat, which possesses in its sequence many pathological fragments. Despite a lot of effort to treat these disorders, the only effective method is a long‐life gluten‐free diet. This Review summarizes the actual knowledge of gluten‐related disorders from a translational chemistry point of view. We discuss what is currently known from the literature about the interaction of gluten with the gut and the critical host responses it evokes and, finally, connect them to our current and novel molecular understanding of the supramolecular organization of gliadin and the 33‐mer gliadin peptide fragment under physiological conditions.

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Self-organization of gliadin in aqueous media under physiological digestive pHs

Cited by 29 publications

References 70 publications

Properties of Gluten Intolerance: Gluten Structure, Evolution, Pathogenicity and Detoxification Capabilities

Properties of Gluten Intolerance: Gluten Structure, Evolution, Pathogenicity and Detoxification Capabilities

Insights into gliadin supramolecular organization at digestive pH 3.0

Translational Chemistry Meets Gluten‐Related Disorders

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