ArticleMolecules (Basel, Switzerland)2021
FT-Raman Spectroscopy as a Tool to Study the Secondary Structures of Wheat Gliadin Proteins.
Article in Molecules (Basel, Switzerland), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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12 citing papers in PubMed, 29 citations in OpenAlex.
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- Applicability of Raman Spectroscopy for the Assessment of Wheat Flour Quality and Functionality in Bakery Applications.Foods (Basel, Switzerland) · 2025Review
- Soil Salinity Differentiates Winter Triticale Genotypes in Physiological and Biochemical Characteristics of Seedlings and Consequently Their Yield.International journal of molecular sciences · 2024Article
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- Study of an arginine- and tryptophan-rich antimicrobial peptide in peri-implantitis.Frontiers in bioengineering and biotechnology · 2024Article
- A Narrative Mini Review on Current Status of Hypoallergenic Wheat Development for IgE-Mediated Wheat Allergy, Wheat-Dependent Exercise-Induced Anaphylaxis.Foods (Basel, Switzerland) · 2023Article
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- The Influence of Biostimulants Used in Sustainable Agriculture for Antifungal Protection on the Chemical Composition of Winter Wheat Grain.International journal of environmental research and public health · 2022Article
- Does Nitrogen Fertilization Affect the Secondary Structures of Gliadin Proteins in Hypoallergenic Wheat?Molecules (Basel, Switzerland) · 2022Article
- Influence of Farming System and Forecrops of Spring Wheat on Protein Content in the Grain and the Physicochemical Properties of Unsonicated and Sonicated Gluten.Molecules (Basel, Switzerland) · 2022Article
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Authors and funding
5 authors at 4 institutions in 1 country.
Funding
Abstract
Raman spectroscopy is a useful method in biological, biomedical, food, and agricultural studies, allowing the simultaneous examination of various chemical compounds and evaluation of molecular changes occurring in tested objects. The purpose of our research was to explain how the elimination of ω-fractions from the wheat gliadin complex influences the secondary structures of the remaining αβγ-gliadins. To this aim, we analyzed the endosperm of wheat kernels as well as gliadin proteins extracted from two winter wheat genotypes: wasko.gl+ (control genotype containing the full set of gliadins) and wasko.gl- (modified genotype lacking all ω-gliadins). Based on the decomposition of the amide I band, we observed a moderate increase in β-forms (sheets and turns) at the expense of α-helical and random coil structures for gliadins isolated from the flour of the wasko.gl- line. Since ω-gliadins contain no cysteine residues, they do not participate in the formation of the disulfide bridges that stabilize the protein structure. However, they can interact with other proteins via weak, low-energetic hydrogen bonds. We conclude that the elimination of ω-fractions from the gliadin complex causes minor modifications in secondary structures of the remaining gliadin proteins. In our opinion, these small, structural changes of proteins may lead to alterations in gliadin allergenicity.
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