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Exploring the Interactions Between Caffeic Acid and Human Serum Albumin Using Spectroscopic and Molecular Docking Techniques
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Kidney Research Center, Tabriz University of Medical Sciences, Tabriz 5166-15731, Iran
Department of Biology, Faculty of Fundamental Sciences, University College of Nabi Akram (UCNA), Tabriz, Iran
Department of Food Sciences, Tabriz Branch, Islamic Azad University, Tabriz, Iran
Drug Applied Research Center, Tabriz University of Medical Sciences, Tabriz, Iran
Department of Food Science and Technology, Faculty of Nutrition and Food Science, Tabriz University of Medical Sciences, Tabriz, Iran
Centro Tecnológico de la Carne de Galicia, Parque Tecnológico de Galicia, 32900 San Cibrao das Viñas, Spain
Área de Tecnología de los Alimentos, Facultad de Ciencias de Ourense, Universidad de Vigo, 32004 Ourense, Spain
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
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
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.
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.
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