Comparison of interaction between three similar chalconoids and α-lactalbumin: Impact on structure and functionality of α-lactalbumin

Food Research International

Volumn 131, Issue , 2020, Pages

  Jiang, Zhanmei ^a   Li, Tianqi ^a   Ma, Ling ^a   Chen, Wei ^a   Yu, Haiying ^a   Abdul, Qayum ^a   Hou, Juncai ^a   Tian, Bo ^a  

^a NORTHEAST AGRICULTURAL UNIVERSITY   (China)

Author keywords

Functionality; Hydroxy safflower yellow A; Interaction; Naringin dihydrochalcone; Neohesperidin dihydrochalcone; Structure; lactalbumin

Indexed keywords

AMINO ACIDS; BINDING ENERGY; EMULSIFICATION; ENERGY TRANSFER; FLAVONOIDS; HYDROGEN BONDS; HYDROPHOBICITY; SPECTRUM ANALYSIS; STRUCTURE (COMPOSITION);

DIHYDROCHALCONE; FUNCTIONAL PROPERTIES; FUNCTIONALITY; HYDROXY SAFFLOWER YELLOW A; INTERACTION; MULTI-SPECTRAL ANALYSIS; NONRADIATIVE ENERGY TRANSFER; SURFACE HYDROPHOBICITY;

FOURIER TRANSFORM INFRARED SPECTROSCOPY;

AURANTIIN; CHALCONE; CHALCONE DERIVATIVE; FLAVANONE DERIVATIVE; HESPERIDIN; LACTALBUMIN; NEOHESPERIDIN; NEOHESPERIDIN DIHYDROCHALCONE; PROTEIN BINDING; SAFFLOWER YELLOW;

ALPHA HELIX; BINDING SITE; CHEMICAL PHENOMENA; CHEMISTRY; EMULSION; HYDROGEN BOND; METABOLISM; MOLECULAR DOCKING;

BINDING SITES; CHALCONE; CHALCONES; EMULSIONS; FLAVANONES; HESPERIDIN; HYDROGEN BONDING; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; LACTALBUMIN; MOLECULAR DOCKING SIMULATION; PROTEIN BINDING; PROTEIN CONFORMATION, ALPHA-HELICAL;

EID: 85078186041     PISSN: 09639969     EISSN: 18737145     Source Type: Journal    
DOI: 10.1016/j.foodres.2020.109006     Document Type: Article

References (62)

1. Al-Hanish, A., Stanic-Vucinic, D., Mihailovic, J., Prodic, I., Minic, S., Stojadinovic, M., Cirkovic, V.T., Noncovalent interactions of bovine α-lactalbumin with green tea polyphenol, epigalocatechin-3-gallate. Food Hydrocolloids 61 (2016), 241–250.
2. Annett, B., Wolfram, E., Michael, B., Degradation of neohesperidin dihydrochalcone by human intestinal bacteria. Journal of Agricultural & Food Chemistry, 53(5), 2005, 1782.
3. Barbana, C., Pérez, M.D., Sánchez, L., Dalgalarrondo, M., Haertlé, T., Chobert, J.M., Calvo, M., Interaction of bovine-lactalbumin with fatty acids as determined by partition equilibrium and fluorescence spectroscopy. International Dairy Journal 16:1 (2006), 18–25.
4. Bi, S., Pang, B., Wang, T., Zhao, T., Yu, W., Investigation on the interactions of clenbuterol to bovine serum albumin and lysozyme by molecular fluorescence technique. Spectrochimica Acta Part A Molecular & Biomolecular Spectroscopy 120:24 (2014), 456–461.
5. Bourassa, P., Côté, R., Hutchandani, S., Samson, G., Tajmirriahi, H.A., The effect of milk alpha-casein on the antioxidant activity of tea polyphenols. Journal of Photochemistry & Photobiology B Biology 128:9 (2013), 43–49.
6. Cao, He Y., Kong, Y., Mei, X., Huo, Y., He, Y., Liu, J., Elucidating the interaction mechanism of eriocitrin with β-casein by multi-spectroscopic and molecular simulation methods. Food Hydrocolloids 94 (2019), 63–70.
7. Cao, Y., Xiong, Y.L., Interaction of whey proteins with phenolic derivatives under neutral and acidic pH conditions. Journal of Food Science 82:2 (2017), 409–419.
8. Carocho, M., & Ferreira, I. C. (2013). A review on antioxidants, prooxidants and related controversy: Natural and synthetic compounds, screening and analysis methodologies and future perspectives. Food & Chemical Toxicology, 51(1), (pp. 15–25).
9. Chandrapala, J., Zisu, B., Palmer, M., Kentish, S., Ashokkumar, M., Effects of ultrasound on the thermal and structural characteristics of proteins in reconstituted whey protein concentrate. Ultrasonics Sonochemistry 18:5 (2011), 951–957.
10. Chrysina E. D., Brew K., & Acharya K. R. (2000). Crystal structures of apo- and holo-bovine alpha-lactalbumin at 2. 2-A resolution reveal an effect of calcium on inter-lobe interactions.
11. Cui, Z., Kong, X., Chen, Y., Zhang, C., Hua, Y., Effects of rutin incorporation on the physical and oxidative stability of soy protein-stabilized emulsions. Food Hydrocolloids 41:20 (2014), 1–9.
12. Dai, T., Chen, J., Mcclements, D.J., Hu, P., Li, T., Protein–polyphenol interactions enhance the antioxidant capacity of phenolics: Analysis of rice glutelin–procyanidin dimer interactions. Food & Function, 10(2), 2019.
13. Dan, Q., Xiong, W., Liang, H., Wu, D., Zhan, F., Chen, Y., Li, B., Characteristic of interaction mechanism between beta-lactoglobulin and nobiletin: A multi-spectroscopic, thermodynamics methods and docking study. Food Reserach International 120 (2019), 255–263.
14. Dubeau, S., Samson, G., Tajmir-Riahi, H.-A., Dual effect of milk on the antioxidant capacity of green, Darjeeling, and English breakfast teas. Food Chemistry 122:3 (2010), 539–545.
15. Frazier, R.A., Deaville, E.R., Green, R.J., Stringano, E., Willoughby, I., Plant, J., Mueller-Harvey, I., Interactions of tea tannins and condensed tannins with proteins. Journal of Pharmaceutical Biomedical Analysis 51:2 (2010), 490–495.
16. Gaudette, N.J., Pickering, G.J., Modifying bitterness in functional food systems. Critical Reviews in Food Science & Nutrition 53:5 (2013), 464–481.
17. Gowda, J.I., Nandibewoor, S.T., Binding and conformational changes of human serum albumin upon interaction with 4-aminoantipyrine studied by spectroscopic methods and cyclic voltammetry. Spectrochim Acta A Molecular Biomolecular Spectroscopy 124:8 (2014), 397–403.
18. Hao, Z., Yu, D., Jing, S., Guo, H., Ding, Q., Liu, R., Ren, F., Interaction of milk whey protein with common phenolic acids. Journal of Molecular Structure 1058:3 (2014), 228–233.
19. Jakobek, & Lidija, (2015). Interactions of polyphenols with carbohydrates, lipids and proteins. Food Chemistry, 175, (pp. 556–567).
20. Janke, C., Jones, R., Coutinho, J., Öberg, S., & Briddon, P. R. (2015). Mobile IMS Integration of the Internet of Things in Ecosystem.
21. Je-Min, C., Byoung-Seok, Y., Sang-Kyou, L., Jae-Kwan, H., Ryung, R., Antioxidant properties of neohesperidin dihydrochalcone: Inhibition of hypochlorous acid-induced DNA strand breakage, protein degradation, and cell death. Biological & Pharmaceutical Bulletin, 30(2), 2007, 324.
22. Jia, J., Gao, X., Hao, M., Tang, L., Comparison of binding interaction between beta-lactoglobulin and three common polyphenols using multi-spectroscopy and modeling methods. Food Chemistry 228 (2017), 143–151.
23. Jiang, Z., Wang, C., Li, T., Sun, D., Gao, H., Gao, Z., Mu, Z., Effect of ultrasound on the structure and functional properties of transglutaminase-crosslinked whey protein isolate exposed to prior heat treatment. International Dairy Journal 88 (2019), 79–88.
24. Kehoe, J.J., Brodkorb, A., Interactions between sodium oleate and α-lactalbumin: The effect of temperature and concentration on complex formation. Food Hydrocolloids 34:1 (2014), 217–226.
25. Kinsella K. N. P. a. J. E. (1978). . Journal of Agricultural and Food Chemistry, 26, (pp. 716–723).
26. Lakowicz, J. R., Freshwater, G., & Weber, G. Nanosecond segmental mobilities of tryptophan residues in proteins observed by lifetime-resolved fluorescence anisotropies. Biophysical Journal.
27. Li, H.P., Dai, T., Li, P., Ye, X., Chen, J., Liu, C., Comparing the binding interaction between β -lactoglobulin and flavonoids with different structure by multi-spectroscopy analysis and molecular docking. Spectrochimica Acta Part A Molecular & Biomolecular Spectroscopy, 201, 2018, 197.
28. Li, Y., Liu, B., Jiang, L., Regenstein, J.M., Jiang, N., Poias, V., Wang, Z., Interaction of soybean protein isolate and phosphatidylcholine in nanoemulsions: A fluorescence analysis. Food Hydrocolloids 87 (2019), 814–829.
29. Li, Y., Liu, H., Liu, Q., Kong, B., Diao, X., Effects of zein hydrolysates coupled with sage (salvia officinalis) extract on the emulsifying and oxidative stability of myofibrillar protein prepared oil-in-water emulsions. Food Hydrocolloids 87 (2019), 149–157.
30. Liu, W., Zhang, Z.Q., Liu, C.M., Xie, M.Y., Tu, Z.C., Liu, J.H., Liang, R.H., The effect of dynamic high-pressure microfluidization on the activity, stability and conformation of trypsin. Food Chemistry 123:3 (2010), 616–621.
31. Livney, Y.D., Milk proteins as vehicles for bioactives. Current Opinion in Colloid & Interface Science 15:1 (2010), 73–83.
32. Manna, A., Chakravorti, S., Role of block copolymer-micelle nanocomposites in dye-bovine serum albumin binding: A combined experimental and molecular docking study. Molecular Biosystems 9:2 (2013), 246–257.
33. Mattia, C.D.D., Sacchetti, G., Mastrocola, D., Sarker, D.K., Pittia, P., Surface properties of phenolic compounds and their influence on the dispersion degree and oxidative stability of olive oil O/W emulsions. Food Hydrocolloids 24:6 (2010), 652–658.
34. Moeiniafshari, A.A., Zarrabi, A., Bordbar, A.K., Exploring the interaction of naringenin with bovine beta-casein nanoparticles using spectroscopy. Food Hydrocolloids 51 (2015), 1–6.
35. Mohammadi, F., Moeeni, M., Analysis of binding interaction of genistein and kaempferol with bovine α-lactalbumin. Journal of Functional Foods 12 (2015), 458–467.
36. Nasr, T., Bondock, S., Eid, S., Design, synthesis, antimicrobial evaluation and molecular docking studies of some new thiophene, pyrazole and pyridone derivatives bearing sulfisoxazole moiety. European Journal of Medicinal Chemistry 84:18 (2014), 491–504.
37. Naveenraj, S., Anandan, S., Binding of serum albumins with bioactive substances – Nanoparticles to drugs. Journal of Photochemistry & Photobiology C Photochemistry Reviews 14:14 (2013), 53–71.
38. Ozdal, T., Capanoglu, E., Altay, F., A review on protein–phenolic interactions and associated changes. Food Research International 51:2 (2013), 954–970.
39. Permyakov, E.A., Berliner, L.J., α-Lactalbumin: Structure and function. Febs Letters 473:3 (2000), 269–274.
40. Perozzo, R., Folkers, G., Scapozza, L., Thermodynamics of protein-ligand interactions: History, presence, and future aspects. Journal of Receptor & Signal Transduction Research 24:1–2 (2004), 1–52.
41. Pinela, J., Prieto, M.A., Carvalho, A.M., Barreiro, M.F., Oliveira, M.B.P.P., Barros, L., Ferreira, I.C.F.R., Microwave-assisted extraction of phenolic acids and flavonoids and production of antioxidant ingredients from tomato: A nutraceutical-oriented optimization study. Separation & Purification Technology 164 (2016), 114–124.
42. Prigent S. V. E., Harry G., Visser A. J. W. G., Koningsveld G. A., Van, Jong G. A. H., De, & Voragen A. G. J. (2003). Effects of non-covalent interactions with 5-O-caffeoylquinic acid (chlorogenic acid) on the heat denaturation and solubility of globular proteins. Journal of Agricultural & Food Chemistry, 51(17), (pp. 5088–5095).
43. Rahman, T.S., Knox, R.S., Kenkre, V.M., Theory of depolarization of fluorescence in molecular pairs ☆. Chemical Physics 44:2 (1979), 197–211.
44. Rawel, H. M., Rohn, S., Kruse, H.P., Kroll, J. (2002). Structural changes induced in bovine serum albumin by covalent attachment of chlorogenic acid. Food Chemistry, 78(4), (pp. 443–455).
45. Ross, P.D., Subramanian, S., Thermodynamics of protein association reactions: Forces contributing to stability. Biochemistry 20:11 (1981), 3096–3102.
46. Seedher, N., Agarwal, P., Complexation of fluoroquinolone antibiotics with human serum albumin: A fluorescence quenching study. Journal of Luminescence 130:10 (2010), 1841–1848.
47. Staszewski, M.V., Ruiz-Henestrosa, V.M.P., Pilosof, A.M.R., Green tea polyphenols-β-lactoglobulin nanocomplexes: Interfacial behavior, emulsification and oxidation stability of fish oil. Food Hydrocolloids 35 (2014), 505–511.
48. Stryer, L., Intramolecular resonance transfer of energy in proteins. Biochimica Et Biophysica Acta 35:1 (1959), 242–244.
49. Sturlese, M., Bellanda, M., Moro, S., NMR-Assisted Molecular Docking Methodologies. Molecular Informatics 34:8 (2015), 513–525.
50. Takase, K., Niki, R., Arima, S., Environment of tryptophan residues in alpha-lactalbumin. Journal of Biochemistry, 83(2), 1978, 371.
51. Tang, L., Li, S., Bi, H., Gao, X., Interaction of cyanidin-3-O-glucoside with three proteins. Food Chemistry 196 (2016), 550–559.
52. Tu, B., Li, R.R., Liu, Z.J., Chen, Z.F., Ouyang, Y., Hu, Y.J., Structure-activity relationship study between baicalein and wogonin by spectrometry, molecular docking and microcalorimetry. Food Chemistry 208 (2016), 192–198.
53. Wang, Z.H., Zhang, G., Zhou, Q., Fei, Z., Liu, Z., Li, Z., Fluorescence spectroscopic investigation of the interaction between benzidine and bovine hemoglobin. Journal of Molecular Structure 886:1–3 (2008), 77–84.
54. Wang, Z.J., Lei, F., Liang, C., Yuan, F., Gao, Y., Covalent complexation and functional evaluation of (−)-epigallocatechin gallate and α-lactalbumin. Food Chemistry 150 (2014), 341–347.
55. Weert, M.V.D., Fluorescence quenching to study protein-ligand binding: common errors. Journal of Fluorescence 20:2 (2010), 625–629.
56. Wei, Z., Wei, Y., Rui, F., Fang, Y., Gao, Y., Evaluation of structural and functional properties of protein–EGCG complexes and their ability of stabilizing a model β-carotene emulsion. Food Hydrocolloids 45 (2015), 337–350.
57. Xu, C., Chen, X., Molecular property-affinity relationship of the interaction between dietary polyphenols and bovine milk proteins. Food & Function 2:7 (2011), 368–372.
58. Yuan, X., Li, X., Zhang, X., Mu, Z., Gao, Z., Jiang, L., Jiang, Z., Effect of ultrasound on structure and functional properties of laccase-catalyzed α-lactalbumin. Journal of Food Engineering 223 (2018), 116–123.
59. Yue, Y., Geng, S., Shi, Y., Liang, G., Wang, J., Liu, B., Interaction mechanism of flavonoids and zein in ethanol-water solution based on 3D-QSAR and spectrofluorimetry. Food Chemistry 276 (2019), 776–781.
60. Zhang, B., Deng, Z., Ramdath, D.D., Tang, Y., Chen, P.X., Liu, R., Rong, T., Phenolic profiles of 20 Canadian lentil cultivars and their contribution to antioxidant activity and inhibitory effects on α-glucosidase and pancreatic lipase. Food Chemistry 172:172C (2015), 862–872.
61. Zhi-Li, W., Jin-Mei, W., Li-Ying, W., Xiao-Quan, Y., Yang, Y., Enhanced physical and oxidative stabilities of soy protein-based emulsions by incorporation of a water-soluble stevioside-resveratrol complex. Journal of Agricultural & Food Chemistry 61:18 (2013), 4433–4440.
62. Zhu, H., Wang, X., Pan, H., Dai, Y., Li, N., Wang, L., …, & Gong. F. (2016). The mechanism by which safflower yellow decreases body fat mass and improves insulin sensitivity in HFD-induced obese mice. Frontiers in Pharmacology, 7.