ReviewBiophysical reviews2018
Gliadins from wheat grain: an overview, from primary structure to nanostructures of aggregates.
Review in Biophysical reviews, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 128 citations in OpenAlex.
- Encapsulation of Protein-Based Drug Carriers for Controlled Loading and Releasing Efficiency: A Review.The protein journal · 2026Review
- Subunit-dependent interfacial assembly of wheat gliadin subunits byFood chemistry: X · 2026Article
- Unraveling the Molecular Interactions Between Ferulic Acid and Wheat Glutenin/Gliadin in Different Systems.Foods (Basel, Switzerland) · 2026Article
- Animal- and Plant-Derived Protein Nanocarriers for the Delivery of Natural Compounds in Breast Cancer Chemoprevention.Molecules (Basel, Switzerland) · 2026Review
- Electrolyte- and Hydrodynamics-Controlled Potentiostatic Growth of Ag Nanodendrites on Metallic Ti for SERS Detection.ACS omega · 2026Article
- Sex-specific effects of cereal-based diets on longevity and healthspan in Drosophila melanogaster.Biogerontology · 2026Article
- Mid-Infrared Spectroscopy for the Qualitative and Quantitative Analysis of the Wheat Proteome.Analytical chemistry · 2026Article
- Influence of commensal bacteria on the proteolytic and antigenic profiles of INFOGEST-like digested wheat gliadin.Frontiers in microbiology · 2026Article
- Texture Evaluation and In Vivo Oral Tactile Perceptions of Cooked Wheat Pasta Sheets Partially Substituted with Pea Protein.Foods (Basel, Switzerland) · 2024Article
- Deciphering the Transcriptional Regulatory Network Governing Starch and Storage Protein Biosynthesis in Wheat for Breeding Improvement.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Wheat-Based Glues in Conservation and Cultural Heritage: (Dis)solving the Proteome of Flour and Starch Pastes and Their Adhering Properties.Journal of proteome research · 2024Article
- Optimizing Gluten Extraction Using Eco-friendly Imidazolium-Based Ionic Liquids: Exploring the Impact of Cation Side Chains and Anions.ACS omega · 2024Article
- 3D-Printable Sustainable Bioplastics from Gluten and Keratin.Gels (Basel, Switzerland) · 2024Article
- Celiac Disease: Risks of Cross-Contamination and Strategies for Gluten Removal in Food Environments.International journal of environmental research and public health · 2024Review
- Insight into Organization of Gliadin and Glutenin Extracted from Gluten Modified by Phenolic Acids.Molecules (Basel, Switzerland) · 2023Article
- Enhancing gluten detection assay development through optimization of gliadin extraction conditions.Heliyon · 2023Article
- The Combination of Gold and Silver Food Nanoparticles with Gluten Peptides Alters the Autophagic Pathway in Intestinal Crypt-like Cells.International journal of molecular sciences · 2023Article
- Insulin Resistance and Hypertension: Mechanisms Involved and Modifying Factors for Effective Glucose Control.Biomedicines · 2023Review
- Functional and Bioactive Properties of Wheat Protein Fractions: Impact of Digestive Enzymes on Antioxidant, α-Amylase, and Angiotensin-Converting Enzyme Inhibition Potential.Molecules (Basel, Switzerland) · 2023Article
- Correlation Analysis between Wheat Flour Solvent Retention Capacity and Gluten Aggregation Characteristics.Foods (Basel, Switzerland) · 2023Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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-L-proline 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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