Molecular Assembly of Wheat Gliadins into Nanostructures: A Small-Angle X-ray Scattering Study of Gliadins in Distilled Water over a Wide Concentration Range

Sato, Nobuhiro; Matsumiya, Aoi; Higashino, Yuki; Funaki, Satoshi; Kitao, Yuki; Oba, Yojiro; Inoue, Rintaro; Arisaka, Fumio; Sugiyama, Masaaki; Urade, Reiko

doi:10.1021/acs.jafc.5b02902

Cited by 20 publications

(27 citation statements)

References 30 publications

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“…By assuming a rod structure for the gliadins at 0.025 wt% in pure water, the shape parameters were calculated to be 10.8 nm long and 7.5 nm in diameter. In analytical ultracentrifugation analysis of gliadins in pure water, the sedimentation coefficient of the major peak, corresponded to a molecular weight of 25.7 kDa, indicating that most of the extracted gliadins were in the monomeric form (Sato et al 2015). Therefore, these differences of Rg and Rc of gliadins may due to the structural difference between gliadins in aqueous ethanol, acidic solutions, and pure water.…”

Section: Size and Shape Of Gliadin Moleculesmentioning

confidence: 99%

“…The amount depended on the concentration of NaCl with which the gluten had been pre-treated (Clements 1973;Fu et al 1996). Ukai et al (2008) and Sato et al (2015) established a method to extract gliadins into pure water from bread dough containing 0.5 M NaCl; the method permitted the extraction of most of the gliadins with few contaminants.…”

Section: Solvent Solubility Of Gliadinsmentioning

confidence: 99%

“…The different results could be due to the proteins adopting different conformations at different degrees of hydration and different pH. Sato et al (2015) performed SAXS analysis of gliadin solution in pure water. The size of gliadin molecules could not be described well by a simple Guinier approximation, even at 0.025 wt%, indicating polydispersity of the scattering components.…”

Section: Size and Shape Of Gliadin Moleculesmentioning

confidence: 99%

“…The SAXS analysis of the structures attained by gliadins over a wide range of their concentrations in aqueous solutions was assessed by Sato et al 2015. A shoulder peak in the SAXS profiles appeared above 1 wt% of the solution (Fig.…”

Section: Aggregated Structures Of Native Gliadinsmentioning

confidence: 99%

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Gliadins from wheat grain: an overview, from primary structure to nanostructures of aggregates

2017

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Gliadins are well-known wheat grain proteins, particularly important in food science. They were studied as early as the 1700s. Despite their long history, it has been difficult to identify their higher-order structure as they aggregate in aqueous solution. Consequently, most studies have been performed by extracting the proteins in 70% ethanol or dilute acidic solutions. The carboxy-terminal half of α-and γ-gliadins have α-helix-rich secondary structures stabilized with intramolecular disulfide bonds, which are present in either aqueous ethanol or pure water. The amino-terminal-repeat region of α-and γ-gliadins has poly-Lproline II and β-reverse-turn structures. ω-Gliadins also have poly-L-proline II and β-reverse-turn structures, but no α-helix structure. The size and shape of gliadin molecules have been determined by assessing a variety of parameters: their sedimentation velocity in the analytical ultracentrifuge, intrinsic viscosity, small-angle X-ray scattering profile, and images of the proteins from scanning probe microscopes such as a tunneling electron microscope and atomic force microscope. Models for gliadins are either rods or prolate ellipsoids whether in aqueous ethanol, dilute acid, or pure water. Recently, gliadins have been shown to be soluble in pure water, and a novel extraction method into pure water has been established. This has made it possible to analyze gliadins in pure water at neutral pH, and permitted the characterization of hydrated gliadins. They formed hierarchical nanoscale structures with internal density fluctuations at high protein concentrations.

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Section: Size and Shape Of Gliadin Moleculesmentioning

confidence: 99%

Section: Solvent Solubility Of Gliadinsmentioning

confidence: 99%

Section: Size and Shape Of Gliadin Moleculesmentioning

confidence: 99%

Section: Aggregated Structures Of Native Gliadinsmentioning

confidence: 99%

See 2 more Smart Citations

Gliadins from wheat grain: an overview, from primary structure to nanostructures of aggregates

2017

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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].…”

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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Aqueous RAFT Synthesis of Low Molecular Weight Anionic Polymers for Determination of Structure/Binding Interactions with Gliadin

Bristol

Carpenter

Davis

et al. 2020

Macromolecular Bioscience

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Gliadin, a component of gluten and a known epitope, is implicated in celiac disease (CeD) and results in an inflammatory response in CeD patients when consumed. Acrylamide-based polyelectrolytes were employed as models to determine the effect of molecular weight and pendent group on non-covalent interaction modes with gliadin in vitro. Poly(sodium 2-acrylamido-2methylpropane sulfonate) and poly(sodium 3-methylpropyl-3-butanoate) were synthesized via aqueous reversible addition fragmentation chain transfer (aRAFT) polymerization and characterized by GPC-MALLS. The polymer/gliadin blends were examined via circular dichroism, zeta potential measurements, ANS fluorescence spectroscopy, and dynamic light scattering. Acrylamide polymers containing strong anionic pendent groups had a profound effect on gliadin secondary structure and solution behavior below the isoelectric point, while polymers containing hydrophobic character only had a minor impact. The polymers had little effect on gliadin secondary structure and solution behavior at the isoelectric point.

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Molecular Assembly of Wheat Gliadins into Nanostructures: A Small-Angle X-ray Scattering Study of Gliadins in Distilled Water over a Wide Concentration Range

Cited by 20 publications

References 30 publications

Gliadins from wheat grain: an overview, from primary structure to nanostructures of aggregates

Gliadins from wheat grain: an overview, from primary structure to nanostructures of aggregates

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

Aqueous RAFT Synthesis of Low Molecular Weight Anionic Polymers for Determination of Structure/Binding Interactions with Gliadin

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