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ORIGINAL ARTICLE
Exploring the Interactions Between Caffeic Acid and Human Serum Albumin Using Spectroscopic and Molecular Docking Techniques
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
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
Corresponding author
Ryszard Amarowicz
Department of Chemical and Physical Properties of Food, Institute of Animal Reproduction and Food Research, Polish Academy of Sciences, Poland
Department of Chemical and Physical Properties of Food, Institute of Animal Reproduction and Food Research, Polish Academy of Sciences, Poland
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.
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Jing Kong, Mingyuan Li, Yutong Li, Min Liu, Qian Zhang, Jie Liu, HongZhuan Xuan
Journal of Molecular Liquids
33.
Investigating sulfonamides - Human serum albumin interactions: A comprehensive approach using multi-spectroscopy, DFT calculations, and molecular docking
Mingguo Peng, Yicui Wang, Chunge Wu, Xuewen Cai, Yao Wu, Erdeng Du, Lu Zheng, Jiajun Fu
Biochemical and Biophysical Research Communications
Mingguo Peng, Yicui Wang, Chunge Wu, Xuewen Cai, Yao Wu, Erdeng Du, Lu Zheng, Jiajun Fu
Biochemical and Biophysical Research Communications
34.
Assessment of the Binding of Pseudallecin A to Human Serum Albumin with Multi‐Spectroscopic Analysis, Molecular Docking and Molecular Dynamic Simulation
Ziyang Li, Ruolan Chen, Chan Qin, Peijun Lu, Jiaru Lin, Wenxu Zheng, Yahong Xiong, Chunyuan Li
Chemistry & Biodiversity
Ziyang Li, Ruolan Chen, Chan Qin, Peijun Lu, Jiaru Lin, Wenxu Zheng, Yahong Xiong, Chunyuan Li
Chemistry & Biodiversity
35.
Thermodynamic and structural investigation of the interaction of quaternized 2,3‐octakis‐[(2‐mercaptopyridine)phthalocyaninato] copper (II) sulfate (CuPc) with parallel and hybrid type G‐quadruplex
Gamze Şahin, Esra Bağda, Temiz Göktuğ, Efkan Bağda, Ebubekir Ayhan, Mahmut Durmuş
Journal of Molecular Recognition
Gamze Şahin, Esra Bağda, Temiz Göktuğ, Efkan Bağda, Ebubekir Ayhan, Mahmut Durmuş
Journal of Molecular Recognition
36.
Spectroscopic and molecular docking investigation on the interaction of a water-soluble Cu(II) complex containing diethanolamine and dipicolinic acid ligands with human serum albumin
Nahid Shahabadi, Azadeh Marzbani, Saba Hadidi, Zahra Mardani
Journal of Biomolecular Structure and Dynamics
Nahid Shahabadi, Azadeh Marzbani, Saba Hadidi, Zahra Mardani
Journal of Biomolecular Structure and Dynamics
37.
Investigating the binding of caffeic acid to human hemoglobin using multispectroscopic and molecular docking approaches
Monika Sharma, Md. Hashmi, Riaz Mahmood
Journal of Molecular Structure
Monika Sharma, Md. Hashmi, Riaz Mahmood
Journal of Molecular Structure
38.
Complexation of bovine lactoferrin with selected phenolic acids via non-covalent interactions: binding mechanism and altered functionality
Cuina Wang, Yingcong Lu, Boxue Xia, Xiang Li, Xin Huang, Chao Dong
Journal of Dairy Science
Cuina Wang, Yingcong Lu, Boxue Xia, Xiang Li, Xin Huang, Chao Dong
Journal of Dairy Science
39.
Analysis on the interaction of coumarin isomers with human serum albumin in the presence of cisplatin
Hongtian Yang, Liang Xu, Yuanhao Liang, Yuan Chen, Yancheng Li, Xiaoying Fan, Yufeng Liu
Journal of Molecular Structure
Hongtian Yang, Liang Xu, Yuanhao Liang, Yuan Chen, Yancheng Li, Xiaoying Fan, Yufeng Liu
Journal of Molecular Structure
40.
Molecularly imprinted polymers for sensing/depleting human serum albumin (HSA): A critical review of recent advances and current challenges
Ali Jahanban-Esfahlan, Ryszard Amarowicz
International Journal of Biological Macromolecules
Ali Jahanban-Esfahlan, Ryszard Amarowicz
International Journal of Biological Macromolecules
41.
Interaction mechanism and compatibility studies of silk protein peptide (SPP) with the common surfactants SDS and DTAB
Qian Zhang, Xinru Zhang, Yaxuan Qi, Yutong Li, Yu Guo, Hanlu Jiang, Yanrong Chen, Jie Liu
Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy
Qian Zhang, Xinru Zhang, Yaxuan Qi, Yutong Li, Yu Guo, Hanlu Jiang, Yanrong Chen, Jie Liu
Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy
42.
A comprehensive investigation of the nano-[Cu2-(DIP)2-EA] effects on HSA through spectroscopic procedures and computer simulations
Nahid Shahabadi, Lida Ghaffari
Heliyon
Nahid Shahabadi, Lida Ghaffari
Heliyon
43.
Inhibitory effect of caffeic acid and dihydrocaffeic acid on the formation of advanced glycation end products: Mechanism analysis based on intermolecular interaction
Yanqing Zhang, Lixia Yuan, Qiulu Wang, Xuejie Zhang, Yiyun Yang, Min Liu
Journal of Molecular Liquids
Yanqing Zhang, Lixia Yuan, Qiulu Wang, Xuejie Zhang, Yiyun Yang, Min Liu
Journal of Molecular Liquids
44.
Dairy and nondairy proteins as nano‐architecture structures for delivering phenolic compounds: Unraveling their molecular interactions to maximize health benefits
Cristine Couto de Almeida, Diego dos Santos Baião, Davi Vieira Teixeira da Silva, Lucileno Rodrigues da Trindade, Patricia Ribeiro Pereira, Carlos Adam Conte‐Junior, Vania Margaret Flosi Paschoalin
Comprehensive Reviews in Food Science and Food Safety
Cristine Couto de Almeida, Diego dos Santos Baião, Davi Vieira Teixeira da Silva, Lucileno Rodrigues da Trindade, Patricia Ribeiro Pereira, Carlos Adam Conte‐Junior, Vania Margaret Flosi Paschoalin
Comprehensive Reviews in Food Science and Food Safety
45.
Optical sensing of albumin in human serum and urine—A historical review of the transition from classical dye-binding assays to advanced technologies
Ali Jahanban-Esfahlan, Ryszard Amarowicz
International Journal of Biological Macromolecules
Ali Jahanban-Esfahlan, Ryszard Amarowicz
International Journal of Biological Macromolecules
| eISSN: | 2083-6007 |
| ISSN: | 1230-0322 |
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