Wheat seed proteins exhibit a complex mechanism of protein elasticity

Tatham, Arthur S.; Hayes, Larry; Shewry, Peter R.; Urry, Dan W.

doi:10.1016/s0167-4838(01)00232-1

Cited by 38 publications

(27 citation statements)

References 22 publications

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“…Tri a 36 belongs to storage proteins, which are important for the germinating seed (35) and accumulate in protein bodies after their synthesis during the seed maturation (36). Accordingly, we found that the amounts of Tri a 36 increased in wheat seeds during maturation and peaked in mature seeds.…”

Section: Discussionmentioning

confidence: 62%

Molecular and Immunological Characterization of Tri a 36, a Low Molecular Weight Glutenin, as a Novel Major Wheat Food Allergen

Baar

Pahr

Constantin

et al. 2012

The Journal of Immunology

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Wheat is an essential element in our nutrition but one of the most important food allergen sources. Wheat allergic patients often suffer from severe gastrointestinal and systemic allergic reactions after wheat ingestion. In this study, we report the molecular and immunological characterization of a new major wheat food allergen, Tri a 36. The cDNA coding for a C-terminal fragment of Tri a 36 was isolated by screening a wheat seed cDNA expression library with serum IgE from wheat food-allergic patients. Tri a 36 is a 369-aa protein with a hydrophobic 25-aa N-terminal leader peptide. According to sequence comparison it belongs to the low m.w. glutenin subunits, which can be found in a variety of cereals. The mature allergen contains an N-terminal domain, a repetitive domain that is rich in glutamine and proline residues, and three C-terminal domains with eight cysteine residues contributing to intra- and intermolecular disulfide bonds. Recombinant Tri a 36 was expressed in Escherichia coli and purified as soluble protein. It reacted with IgE Abs of ∼80% of wheat food-allergic patients, showed IgE cross-reactivity with related allergens in rye, barley, oat, spelt, and rice, and induced specific and dose-dependent basophil activation. Even after extensive in vitro gastric and duodenal digestion, Tri a 36 released distinct IgE-reactive fragments and was highly resistant against boiling. Thus, recombinant Tri a 36 is a major wheat food allergen that can be used for the molecular diagnosis of, and for the development of specific immunotherapy strategies against, wheat food allergy.

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Section: Discussionmentioning

confidence: 62%

Molecular and Immunological Characterization of Tri a 36, a Low Molecular Weight Glutenin, as a Novel Major Wheat Food Allergen

Baar

Pahr

Constantin

et al. 2012

The Journal of Immunology

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“…As for the random coil, it increased by 28.61 %. The reason why both intramolecular β-sheet and α-helix were decreased was probably due to CFU pretreatment was weakened the interaction of gliadins and glutenin and reduced the internal disulfide bonds and polar hydrogen bonding [34,35]. The content of random coil was higher in the CFU pretreatment sample, it revealed that the secondary institutions of wheat gluten were more disordered and stretching attributed to CFU pretreatment.…”

Section: Ftir Spectroscopic Characterizationmentioning

confidence: 93%

Effects of Ultrasound Pretreatment on the Enzymolysis and Structural Characterization of Wheat Gluten

Zhang

Wang

et al. 2015

Food Biophysics

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Ultrasound pretreatment of protein could improve the angiotensin-I converting enzyme (ACE) inhibitory activity of hydrolysates and by alerting the structure of enzyme substrates. In this research the effects on ACE inhibitory activity and enzymolysis efficiency were explored under the optimum counter flow ultrasound (CFU) pretreatment conditions which obtained from our previous studies. The mechanism was studied by microstructure, nano-mechanical properties and secondary structures of wheat gluten (WG), which measured by scanning electron microscopy (SEM), atomic force microscopy (AFM), and flourier transform infrared spectrum (FTIR). The results showed that the CFU pretreatment resulted in significantly (P<0.05) higher value compared with control, the ACE inhibitory activity was increased by 29.8 % and the value of IC 50 was decreased by 36.92 %. CFU pretreatment increased the initial reaction rate by 9.58-20.27 % at a substrate concentration of 10-50 g/L, the K A was increased by 2.90 % and K M was decreased by 15.83 % compared to control. The microstructure revealed that the meshwork structure of WG was loosened and the surface roughness values of R a and R q were increased by CFU pretreatment. The nanomechanical analyses showed that CFU pretreatment redistributed the adhesion map and decreased the stiffness. The secondary structures were less ordered by CFU pretreatment. Intermolecular β-sheet of protein aggregation and random coil were increased, Intramolecular β-sheet, α-helix and β-turn were decreased. It was concluded that CFU pretreatment can remarkably improve the ACE inhibitory activity of hydrolysate and enzymolysis efficiency of WG confirmed by the changes of microstructure, nano-mechanical properties, and secondary structures.

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“…[4][5][6] even though many other elastomeric proteins are described, such as spider silk fibroin, [7,8] byssus and abductin [9,10] from bivalve mollusks, resilin from arthropods [11] and gluten from wheat. [12] Although the elastomeric proteins are widely distributed and exhibit unique mechanical characteristics, only a few have been structurally characterised in detail. For example, various molecular and biological data are available for the elasticity of elastin thanks to several studies on biological samples of elastin from tissues and on elastinderived peptides, whereas much less information is known about other remarkable elastomeric proteins.…”

Section: Introductionmentioning

confidence: 99%

Molecular and Supramolecular Structural Studies on Significant Repetitive Sequences of Resilin

et al. 2009

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Resilin is a member of the family of elastomeric proteins and is found in specialised regions of the cuticle of most insects, and provides low stiffness, high strain and efficient energy storage. It is best known for its role in insect flight and the remarkable jumping ability of fleas and spittle bugs. In common with other elastomeric proteins, the recently identified Drosophila melanogaster proresilin shows glycine-rich repetitive sequences; in particular the N- and C-terminal regions of the protein are dominated by 18 repeats of a 15-residue sequence (SDTYGAPGGGNGGRP) and eleven repeats of a 13-residue sequence (GYSGGRPGGQDLG), respectively. We synthesised and analysed the molecular and supramolecular structure of some polypeptides with sequences belonging to the glycine-rich repeated domain of D. melanogaster resilin. The conformational studies performed by CD, FTIR and NMR spectroscopies pointed to the coexistence of two main conformational features, such as folded beta-turns and (quasi)extended structures (e.g., poly-L-proline II conformation) in common with other elastomeric proteins; this suggests an elasticity mechanism for resilin common to other elastomeric proteins. Our data show that also in the case of resilin, repetitive sequences are characterised by autonomous structures almost independent of the remaining parts of the molecule as already extensively found for elastin. From a supramolecular point of view, a great tendency to aggregate in fibrous structures is observed, particularly for the resilin- inspired polypeptide (PGGGN)(10). This is encouraging for the development of resilin-based biomaterials for the production of biocompatible medical devices, as well as high performing elastic materials.

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Wheat seed proteins exhibit a complex mechanism of protein elasticity

Cited by 38 publications

References 22 publications

Molecular and Immunological Characterization of Tri a 36, a Low Molecular Weight Glutenin, as a Novel Major Wheat Food Allergen

Molecular and Immunological Characterization of Tri a 36, a Low Molecular Weight Glutenin, as a Novel Major Wheat Food Allergen

Effects of Ultrasound Pretreatment on the Enzymolysis and Structural Characterization of Wheat Gluten

Molecular and Supramolecular Structural Studies on Significant Repetitive Sequences of Resilin

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