Search for Author, Title, Keyword
ORIGINAL ARTICLE
Exploring the Interactions Between Caffeic Acid and Human Serum Albumin Using Spectroscopic and Molecular Docking Techniques
 
More details
Hide details
1
Kidney Research Center, Tabriz University of Medical Sciences, Tabriz 5166-15731, Iran
2
Department of Biology, Faculty of Fundamental Sciences, University College of Nabi Akram (UCNA), Tabriz, Iran
3
Department of Food Sciences, Tabriz Branch, Islamic Azad University, Tabriz, Iran
4
Drug Applied Research Center, Tabriz University of Medical Sciences, Tabriz, Iran
5
Department of Food Science and Technology, Faculty of Nutrition and Food Science, Tabriz University of Medical Sciences, Tabriz, Iran
6
Centro Tecnológico de la Carne de Galicia, Parque Tecnológico de Galicia, 32900 San Cibrao das Viñas, Spain
7
Área de Tecnología de los Alimentos, Facultad de Ciencias de Ourense, Universidad de Vigo, 32004 Ourense, Spain
8
Department of Chemical and Physical Properties of Food, Institute of Animal Reproduction and Food Research of the Polish Academy of Sciences, Tuwima 10, 10-486 Olsztyn, Poland
CORRESPONDING AUTHOR
Ryszard Amarowicz   

Department of Chemical and Physical Properties of Food, Institute of Animal Reproduction and Food Research, Polish Academy of Sciences, Poland
Submission date: 2020-12-10
Final revision date: 2021-02-08
Acceptance date: 2021-02-10
Online publication date: 2021-02-24
Publication date: 2021-02-24
 
Pol. J. Food Nutr. Sci. 2021;71(1):69–77
 
KEYWORDS
TOPICS
ABSTRACT
Ultraviolet-visible (UV–Vis) and fluorescence spectroscopy along with molecular docking were used to explore the interaction between human serum albumin (HSA) and caffeic acid (CA). CA is one of the major representatives of hydroxycinnamic acids in plants and is commonly present in plant-based foods. The mechanism by which CA quenched HSA fluorescence was determined to be static, and the values obtained for thermodynamic parameters indicated that the CA and HSA interaction was spontaneous. Hydrogen bonds and van der Waals forces were the main driving forces stabilizing the complex. The binding constant was in the order of 104/M and the number of binding sites for CA on HSA was calculated to be close to one. The results of fluorescence and UV–Vis spectroscopy showed that CA induced conformational changes in HSA structure. The distance of CA and the tryptophan residue of HSA, was determined to be ~2 nm by using Forster resonance energy transfer theory. The mode of binding and the binding site of CA on albumin were examined by performing molecular docking calculations. CA interacted with albumin in subdomain IA, and non–covalent interactions stabilized the complex. CA showed a high affinity for albumin, and thus this phenolic compound would be distributed in the body upon interacting with HSA.
ABBREVIATIONS
CA – caffeic acid; FRET – Forster resonance energy transfer; H–bonds – hydrogen bonds; HCAs – hydroxycinnamic acids; HAS – human serum albumin; IFE – internal filter effect; SV – Stern–Volmer; UV–Vis – ultraviolet-visible; and vdW – van der Waals.
 
REFERENCES (45)
1.
Adzet, T., Camarasa, J., Escubedo, E., Merlos, M. (1988). In vitro study of caffeic acid - bovine serum albumin interaction. European Journal of Drug Metabolism and Pharmacokinetics, 13(1), 11-14. https://doi.org/10.1007/BF0318....
 
2.
Belatik, A., Hotchandani, S., Bariyanga, J., Tajmir-Riahi, H. (2012). Binding sites of retinol and retinoic acid with serum albumins. European Journal of Medicinal Chemistry, 48, 114-123. https://doi.org/10.1016/j.ejme....
 
3.
Bhat, S., Azmi, A., Hadi, S. (2007). Prooxidant DNA breakage induced by caffeic acid in human peripheral lymphocytes: Involvement of endogenous copper and a putative mechanism for anticancer properties. Toxicology and Applied Pharmacology, 218(3), 249-255. https://doi.org/10.1016/j.taap....
 
4.
Bourassa, P., Hasni, I., Tajmir-Riahi, H. (2011). Folic acid complexes with human and bovine serum albumins. Food Chemistry, 129(3), 1148-1155. https://doi.org/10.1016/j.food....
 
5.
Chen, G.-Z., Huang, X.-Z., Xu, J.-G., Zheng, Z., Wang, Z. (1990). The Methods of Fluorescence Analysis. 2nd edition, Science Press, Beijing, pp.112-117.
 
6.
Chen, J.H., Ho, C.-T. (1997). Antioxidant activities of caffeic acid and its related hydroxycinnamic acid compounds. Journal of Agricultural and Food Chemistry, 45(7), 2374-2378. https://doi.org/10.1021/jf9700....
 
7.
Chung, M., Walker, P., Hogstrand, C. (2006). Dietary phenolic antioxidants, caffeic acid and Trolox, protect rainbow trout gill cells from nitric oxide-induced apoptosis. Aquatic Toxicology, 80(4), 321-328. https://doi.org/10.1016/j.aqua....
 
8.
Cui, F.-L., Fan, J., Li, J.-P., Hu, Z.-D. (2004). Interactions between 1-benzoyl-4-p-chlorophenyl thiosemicarbazide and serum albumin: investigation by fluorescence spectroscopy. Bioorganic & Medicinal Chemistry, 12(1), 151-157. https://doi.org/10.1016/j.bmc.....
 
9.
Dan, Q., Xiong, W., Liang, H., Wu, D., Zhan, F., Chen, Y., Ding, Li, B. (2019). Characteristic of interaction mechanism between β-lactoglobulin and nobiletin: A multi-spectroscopic, thermodynamics methods and docking study. Food Research International, 120, 255-263. https://doi.org/10.1016/j.food....
 
10.
Eftink, M.R. (1991). Fluorescence quenching reactions: Probing biological macromolecular structures. In T.G. Dewey (Ed.). Biophysical and Biochemical Aspects of Fluorescence Spectroscopy. 1st edition, Springer Science + Business Media LCC, New York, USA, chapter 1, pp. 1-42. https://doi.org/10.1007/978-1-...
 
11.
El-Seedi, H.R., El-Said, A.M.A. Khalifa, S.A.M., Göransson, U., Bohlin, L., Borg-Karlson, A.-K., Verpoorte, R. (2012). Biosynthesis, natural sources, dietary intake, pharmacokinetic properties, and biological activities of hydroxycinnamic acids. Journal of Agricultural and Food Chemistry, 60(44), 10877-10895. https://doi.org/10.1021/jf3018....
 
12.
Jahanban-Esfahlan, A., Dastmalchi, S., Davaran, S. (2016). A simple improved desolvation method for the rapid preparation of albumin nanoparticles. International Journal of Biomolecular Macromolecules, 91, 703-709. https://doi.org/10.1016/j.ijbi....
 
13.
Jahanban-Esfahlan, A., Davaran, S., Moosavi-Movahedi, A.A., Dastmalchi, S. (2017). Investigating the interaction of juglone (5-hydroxy-1,4-naphthoquinone) with serum albumins using spectroscopic and in silico methods. Journal of the Iranian Chemical Society, 14, 1527-1540. https://doi.org/10.1007/s13738....
 
14.
Jahanban-Esfahlan, A., Ostadrahimi, A., Jahanban-Esfahlan, R., Roufegarinejad, L., Tabibiazar, M., Amarowicz, R. (2019). Recent developments in the detection of bovine serum albumin. International Journal of Biomolecular Macromolecules,138, 602-617. https://doi.org/10.1016/j.ijbi....
 
15.
Jahanban-Esfahlan, A., Panahi-Azar, V., Sajedi, S. (2015). Spectroscopic and molecular docking studies on the interaction between N-acetyl cysteine and bovine serum albumin. Biopolymers, 103, 638-645. https://doi.org/10.1002/bip.22....
 
16.
Jahanban-Esfahlan, A., Roufegarinejad, L., Jahanban-Esfahlan, R., Tabibiazar, M., Amarowicz, R. (2020). Latest developments in the detection and separation of bovine serum albumin using molecularly imprinted polymers. Talanta, 207, art. no. 120317. https://doi.org/10.1016/j.tala....
 
17.
Lakowicz, J.R. (2006). Principles of Fluorescence Spectroscopy. 3rd edition, Springer Science + Business Media, New York, USA, chapter 13, pp. 443-452. https://doi.org/10.1007/978-0-....
 
18.
Lakowicz, J.R., Weber, G. (1973). Quenching of fluorescence by oxygen. Probe for structural fluctuations in macromolecules. Biochemistry, 12(21), 4161-4170. https://doi.org/10.1021/bi0074....
 
19.
Lehrer, S. (1971). Solute perturbation of protein fluorescence. Quenching of the tryptophyl fluorescence of model compounds and of lysozyme by iodide ion. Biochemistry, 10(17), 3254-3263. https://doi.org/10.1021/bi0079....
 
20.
Li, S., Huang, K., Zhong, M., Guo, J., Wang, W.-Z., Zhu, R. (2010). Comparative studies on the interaction of caffeic acid, chlorogenic acid and ferulic acid with bovine serum albumin. Spectrochimica Acta, Part A: Molecular and Biomolecular Spectroscopy, 77(3), 680-686. https://doi.org/10.1016/j.saa.....
 
21.
Min, J., Meng-Xia, X., Dong, Z., Yuan, L., Xiao-Yu, L., Xing, C. (2004). Spectroscopic studies on the interaction of cinnamic acid and its hydroxyl derivatives with human serum albumin. Journal of Molecular Structures, 692(1-3), 71-80. https://doi.org/10.1016/j.mols....
 
22.
Mrkalić, E., Jelićb, R., Stojanović, S., Sovrlić, M. (2021). Interaction between olanzapine and human serum albumin and effect of metal ions, caffeine and flavonoids on the binding: A spectroscopic study. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 249, art. no. 119295. https://doi.org/10.1016/j.saa.....
 
23.
Nair, M.S. (2018). Spectroscopic studies on the interaction of serum albumins with plant derived natural molecules. Applied Spectroscopy Reviews, 53(8), 636-666. https://doi.org/10.1080/057049....
 
24.
Olthof, M.R., Hollman, P. C.-H., Katan, M.B. (2001). Chlorogenic acid and caffeic acid are absorbed in humans. The Journal of Nutrition, 131(1), 66-71. https://doi.org/10.1093/jn/131....
 
25.
Pirjo, M., Hellström, J., Törrönen, R. (2006). Phenolic acids in berries, fruits, and beverages. Journal of Agricultural and Food Chemistry, 53(19), 7193-7199. https://doi.org/10.1021/jf0615....
 
26.
Precupas, A., Sandu, R., Cantemir, A.R., Anghel, D.-F., Popa, V.T. (2017). Interaction of caffeic acid with bovine serum albumin is complex: Calorimetric, spectroscopic and molecular docking evidence. New Journal of Chemistry, 41, 15003-15015. https://doi.org/10.1039/C7NJ03....
 
27.
Rashmi, H.B., Negi, P.S. (2020). Phenolic acids from vegetables: A review on processing stability and health benefits. Food Research International, 136, art. no. 109298. https://doi.org/10.1016/j.food....
 
28.
Razzak M.A., Lee, J.-E., Choi, S.S. (2019). Structural insights into the binding behavior of isoflavonoid glabridin with human serum albumin. Food Hydrocolloids, 91, 290-300. https://doi.org/10.1016/j.food....
 
29.
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....
 
30.
Roufegarinejad, L., Amarowicz, R., Jahanban-Esfahlan, A. (2019). Characterizing the interaction between pyrogallol and human serum albumin by spectroscopic and molecular docking methods. Journal of Biomolecular Structure and Dynamics, 37(11), 2766-2775. https://doi.org/10.1080/073911....
 
31.
Samari, F., Shamsipur, M., Hemmateenejad, B., Khayamian, T., Gharaghani, S. (2012). Investigation of the interaction between amodiaquine and human serum albumin by fluorescence spectroscopy and molecular modeling. European Journal of Medicinal Chemistry, 54, 255-263. https://doi.org/10.1016/j.ejme....
 
32.
Sinisi, V., Forzato, C., Cefarin, N., Navarini, L., Berti, F. (2015). Interaction of chlorogenic acids and quinides from coffee with human serum albumin. Food Chemistry, 168, 332-340. https://doi.org/10.1016/j.food....
 
33.
Skrt, M., Benedik, E., Podlipnik, C., Ulrih, N.P. (2012). Interactions of different polyphenols with bovine serum albumin using fluorescence quenching and molecular docking. Food Chemistry, 135, 2418–2424. https://doi.org/10.1016/j.food....
 
34.
Sova, M., Saso, L. (2020). Natural sources, pharmacokinetics, biological activities and health benefits of hydroxycinnamic acids and their metabolites. Nutrients, 12(8), art. no. 2190. https://doi.org/10.3390/nu1208....
 
35.
Sułkowska, A. (2002). Interaction of drugs with bovine and human serum albumin. Journal of Molecular Structure, 614(1-3), 227-232. https://doi.org/10.1016/S0022-...
 
36.
Suryaprakash, P., Kumar, R.P., Prakash, V. (2000). Thermodynamics of interaction of caffeic acid and quinic acid with multisubunit proteins. International Journal of Biological Macromolecules, 27(3), 219-228. https://doi.org/10.1016/S0141-....
 
37.
Sun, Q., Yang, H., Tang, P., Liu, J., Wang, W., Li, H. (2018). Interactions of cinnamaldehyde and its metabolite cinnamic acid with human serum albumin and interference of other food additives. Food Chemistry, 243, 74-81. https://doi.org/10.1016/j.food....
 
38.
Sudhamalla, B., Gokara, M., Ahalawat, N., Amooru, D.G., Subramanyam, R. (2010). Molecular dynamics simulation and binding studies of β-sitosterol with human serum albumin and its biological relevance. Journal of Physical Chemistry, 114(27), 9054-9062. https://doi.org/10.1021/jp1027....
 
39.
Tomašević, M., Lisjak, K., Vanzo, A., Ganić, K.K. (2019). Changes in the composition of aroma and phenolic compounds induced by different enological practices of Croatian white wine. Polish Journal of Food and Nutrition Sciences, 69(4), 343-358. https://doi.org/10.31883/pjfns....
 
40.
Ulrich, K.-H. (1981). Molecular aspects of ligand binding to serum albumin. Pharmacological Reviews, 33(1), 17-53.
 
41.
Ulrich, K.-H. (1990). Structure and ligand binding properties of human serum albumin. Danish Medical Bulletin, 37(1), 57-84.
 
42.
Wang, N., Ye, L., Yan, F., Xu, R. (2008). Spectroscopic studies on the interaction of azelnidipine with bovine serum albumin. International Journal of Pharmaceutics, 351(1-2), 55-60. https://doi.org/10.1016/j.ijph....
 
43.
Worldwide Protein Data Bank (wwPDB). Available online: [https://www.rcsb.org/structure...] (accessed on 10 April 2020).
 
44.
Zhang, Y., Yue, Y., Li, J., Chen, X. (2008). Studies on the interaction of caffeic acid with human serum albumin in membrane mimetic environments. Journal of Photochemistry and Photobiology B: Biology, 90(3), 141-151. https://doi.org/10.1016/j.jpho....
 
45.
Zou, Y.-C., Wu, C.-L., Ma, C.-F., He, S., Brennan, C.S., Yuan, Y. (2019). Interactions of grape seed procyanidins with soy protein isolate: Contributing antioxidant and stability properties. LWT – Food Science and Technology, 115, art. no. 108465. https://doi.org/10.1016/j.lwt.....
 
 
CITATIONS (2):
1.
Effect of local anesthetic drug procaine hydrochloride on the conformational stability of bovine hemoglobin: Multi-spectroscopic and computational approaches
Deepak Kaushal, Hira Lal, Sameer Ansari, Saeeda Naqvi
Journal of Biomolecular Structure and Dynamics
 
2.
Probing the interaction of fisetin with human serum transferrin via spectroscopic and molecular docking approaches
Nicoleta Sandu, Aurel Popescu, Claudia Chilom
Journal of Biomolecular Structure and Dynamics
 
eISSN:2083-6007
ISSN:1230-0322