RESEARCH PAPER
Gliadins as a potential carrier of health-promoting phenolic acids: fluorescence study of gliadin – phenolic acids complexation
1
Institute of Agrophysics, Polish Academy of Sciences, Doświadczalna 4, 20-290 Lublin, Poland
2
Department of Plant Physiology and Biophysics, Institute of Biological Sciences, Maria Curie-Skłodowska University, Akademicka 19, 20-033 Lublin, Poland
Final revision date: 2024-12-04
Acceptance date: 2024-12-16
Publication date: 2025-04-28
Corresponding author
Renata Welc-Stanowska
Department of Plant Physiology and Biophysics, Maria Curie-Skłodowska University, Poland
Department of Plant Physiology and Biophysics, Maria Curie-Skłodowska University, Poland
Int. Agrophys. 2025, 39(3): 245-253
HIGHLIGHTS
- Phenolic acids quench gliadin fluorescence by complexes formation
- Phenolic acids are bond reversibly and exhibit moderate affinities to protein
- Caffeic, ferulic and sinapic acids interact with gliadin to form 1:1 complexes
- Hydrogen bonding play major role in the phenolic acids-gliadin complexation
KEYWORDS
TOPICS
ABSTRACT
Due to the health benefits attributed to the consumption of phenolic acids, these compounds can be used as natural pro-health food or beverages ingredients. To improve polyphenols stability during food processing and storage, they could be encapsulated in colloidal systems e.g. via complexation with proteins. The process of gliadin protein and phenolic acids complexation was investigated with application of fluorescence spectroscopy. Strong fluorescence quenching of gliadin was observed as a result of phenolic addition and two types of quenching mechanism were determined: dynamic (for coumaric acid) and static (for caffeic, ferulic and sinapic acid). This result indicates that coumaric acid, unlike to other analysed acids, does not form complexes with gliadin. The binding constant for caffeic, ferulic and sinapic acid – gliadin interaction is between 0.4 and 8.7 x 103 M-1. These three acids induced changes in protein conformation and tryptophan microenvironment. The calculated number of binding sites suggests that caffeic, ferulic and sinapic acids interact with gliadin to form 1:1 complexes. Analysis of thermodynamic parameters suggested that van der Waals and/or hydrogen bonding interactions play major role in the interactions between caffeic, ferulic as well as sinapic acid and gliadin.
FUNDING
This work was supported by the National Science Centre, Poland (grant number: 2019/35/B/NZ9/02854).
CONFLICT OF INTEREST
The Authors do not declare any conflict of interest.
REFERENCES (28)
1.
Acharya, D.P., Sanguansri, L., Augustin, M.A., 2013. Binding of resveratrol with sodium caseinate in aqueous solutions. Food Chem, 141(2), 1050-1054. https://doi.org/10.1016/j.food....
2.
Albani, J.R., 2014a. Origin of tryptophan fluorescence lifetimes Part 1. Fluorescence lifetimes origin of tryptophan free in solution. J. Fluorescence 24(1), 93-104. https://doi.org/10.1007/s10895....
3.
Albani, J.R., 2014b. Origin of tryptophan fluorescence lifetimes. Part 2: Fluorescence lifetimes origin of tryptophan in proteins. J. Fluorescence 24(1), 105-117. https://doi.org/10.1007/s10895....
4.
Barak, S., Mudgil, D., Khatkar, B.S., 2015. Biochemical and functional properties of wheat gliadins: A Review. Critical Reviews in Food Science and Nutrition 55(3), 357-368. https://doi.org/10.1080/104083....
5.
Butkus, J.M., O’Riley, S., Chohan, B.S., Basu, S., 2016. Interaction of small zinc complexes with globular proteins and free tryptophan. Int. J. Spectroscopy 2016, e1378680. https://doi.org/10.1155/2016/1....
6.
Dias, R., Perez-Gregorio, R., Mateus, N., Freitas, V.D., 2015. The interaction between tannins and gliadin derived peptides in a celiac disease perspective. RSC Advances, 5(41), 32151-32158. https://doi.org/10.1039/C5RA02....
7.
Dufour, C., Dangles, O., 2005. Flavonoid-serum albumin complexation: Determination of binding constants and binding sites by fluorescence spectroscopy. Biochimica et Biophysica Acta (BBA) – General Subjects, 1721(1), 164-173. https://doi.org/10.1016/j.bbag....
8.
Ghali, M., 2010. Static quenching of bovine serum albumin conjugated with small size CdS nanocrystalline quantum dots. J. Luminescence 130(7), 1254-1257. https://doi.org/10.1016/j.jlum....
9.
Joye, I.J., Davidov-Pardo, G., Ludescher, R.D., McClements, D.J., 2015. Fluorescence quenching study of resveratrol binding to zein and gliadin: Towards a more rational approach to resveratrol encapsulation using water-insoluble proteins. Food Chemistry 185, 261-267. https://doi.org/10.1016/j.food....
10.
Karasawa, M.M.G., Mohan, C., 2018. Fruits as prospective reserves of bioactive compounds: A Review. Natural Products and Bioprospecting 8(5), 335-346. https://doi.org/10.1007/s13659....
11.
Kłosok, K., Welc, R., Fornal, E., Nawrocka, A., 2021. Effects of Physical and chemical factors on the structure of gluten, gliadins and glutenins as studied with spectroscopic methods. Molecules 26(2), Article 2. https://doi.org/10.3390/molecu....
12.
Kłosok, K., Welc, R., Szymańska-Chargot, M., Nawrocka, A., 2022. Phenolic acids-induced aggregation of gluten proteins. Structural analysis of the gluten network using FT-Raman spectroscopy. J. Cereal Sci. 107, 103503. https://doi.org/10.1016/j.jcs.....
13.
Krekora, M., Szymańska-Chargot, M., Niewiadomski, Z., Miś, A., Nawrocka, A., 2020. Effect of cinnamic acid and its derivatives on structure of gluten proteins – A study on model dough with application of FT-Raman spectroscopy. Food Hydrocolloids 107, 105935. https://doi.org/10.1016/j.food....
14.
Lakowicz, J.R., 2006. Principles of Fluorescence Spectroscopy (3rd ed.). Kluwer Academic/Plenum Publishers.
15.
Liang, L., Tajmir-Riahi, H.A., Subirade, M., 2008. Interaction of beta-lactoglobulin with resveratrol and its biological implications. Biomacromolecules 9(1), 50-56. https://doi.org/10.1021/bm7007....
16.
Pérot, M., Lupi, R., Guyot, S., Delayre-Orthez, C., Gadonna-Widehem, P., Thébaudin, J.-Y., Bodinier, M., Larré, C., 2017. Polyphenol interactions mitigate the immunogenicity and allergenicity of gliadins. J. Agric. Food Chem. 65(31), 6442-6451. https://doi.org/10.1021/acs.ja....
17.
Rashmi, H.B., Negi, P.S., 2020. Phenolic acids from vegetables: A review on processing stability and health benefits. Food Research Int. 136, 109298. https://doi.org/10.1016/j.food....
18.
Ross, P.D., Subramanian, S., 1981. Thermodynamics of protein association reactions: Forces contributing to stability. Biochemistry 20(11), 3096-3102. https://doi.org/10.1021/bi0051....
19.
Sivam, A.S., Sun-Waterhouse, D., Quek, S., Perera, C.O., 2010. Properties of bread dough with added fiber polysaccharides and phenolic antioxidants: A Review. J. Food Sci. 75(8), R163-R174. https://doi.org/10.1111/j.1750....
20.
Stuper-Szablewska, K., Perkowski, J., 2019. Phenolic acids in cereal grain: Occurrence, biosynthesis, metabolism and role in living organisms. Critical Reviews in Food Sci. Nutrition 59(4), 664-675. https://doi.org/10.1080/104083....
21.
Tsao, R., Deng, Z., 2004. Separation procedures for naturally occurring antioxidant phytochemicals. J. Chromatography. B, Analytical Technologies in the Biomedical and Life Sci. 812(1-2), 85-99. https://doi.org/10.1016/j.jchr....
22.
Urade, R., Sato, N., Sugiyama, M., 2017. Gliadins from wheat grain: An overview, from primary structure to nanostructures of aggregates. Biophysical Reviews 10(2), 435-443. https://doi.org/10.1007/s12551....
23.
Wang, G., Chen, Y., Yan, C., Lu, Y., 2015. Study on the interaction between gold nanoparticles and papain by spectroscopic methods. J. Luminescence 157, 229-234. https://doi.org/10.1016/j.jlum....
24.
Wang, Q., Tang, Y., Yang, Y., Zhao, J., Zhang, Y., Li, L., Wang, Q., Ming, J., 2020. Interaction between wheat gliadin and quercetin under different pH conditions analyzed by multi-spectroscopy methods. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy 229, 117937. https://doi.org/10.1016/j.saa.....
25.
Welc, R., Kłosok, K., Szymańska-Chargot, M., Nawrocka, A., 2022a. Effect of chemical structure of selected phenolic acids on the structure of gluten proteins. Food Chem. 389, 133109. https://doi.org/10.1016/j.food....
26.
Welc, R., Luchowski, R., Kłosok, K., Gruszecki, W.I., Nawrocka, A., 2022b. How do phenolic acids change the secondary and tertiary structure of gliadin? Studies with an Application of Spectroscopic Techniques. Int. J. Molecular Sci. 23(11), 6053. https://doi.org/10.3390/ijms23....
27.
Xiao, J., Mao, F., Yang, F., Zhao, Y., Zhang, C., Yamamoto, K., 2011. Interaction of dietary polyphenols with bovine milk proteins: Molecular structure-affinity relationship and influencing bioactivity aspects. Molecular Nutrition Food Res. 55(11), 1637-1645. https://doi.org/10.1002/mnfr.2....
28.
Ye, J.-H., Thomas, E., Sanguansri, L., Liang, Y.-R., Augustin, M.A., 2013. Interaction between Whole Buttermilk and Resveratrol. J. Agric. Food Chem. 61(29), 7096-7101. https://doi.org/10.1021/jf4017....
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