Exploring the Interactions Between Caffeic Acid and Human Serum Albumin Using Spectroscopic and Molecular Docking Techniques
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...
Saved in:
| Main Authors: | , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Institute of Animal Reproduction and Food Research of the Polish Academy of Sciences
2021-02-01
|
| Series: | Polish Journal of Food and Nutrition Sciences |
| Subjects: | |
| Online Access: | http://journal.pan.olsztyn.pl/Exploring-the-Interactions-Between-Caffeic-Acid-and-Human-Serum-Albumin-Using-Spectroscopic,133203,0,2.html |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| _version_ | 1832557792331825152 |
|---|---|
| author | Ali Jahanban-Esfahlan Leila Roufegarinejad Mahnaz Tabibiazar José M. Lorenzo Ryszard Amarowicz |
| author_facet | Ali Jahanban-Esfahlan Leila Roufegarinejad Mahnaz Tabibiazar José M. Lorenzo Ryszard Amarowicz |
| author_sort | Ali Jahanban-Esfahlan |
| collection | DOAJ |
| description | 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 10 4 /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. |
| format | Article |
| id | doaj-art-c586e58e69624221aa01c0ca3ab89f71 |
| institution | Kabale University |
| issn | 2083-6007 |
| language | English |
| publishDate | 2021-02-01 |
| publisher | Institute of Animal Reproduction and Food Research of the Polish Academy of Sciences |
| record_format | Article |
| series | Polish Journal of Food and Nutrition Sciences |
| spelling | doaj-art-c586e58e69624221aa01c0ca3ab89f712025-02-03T02:24:15ZengInstitute of Animal Reproduction and Food Research of the Polish Academy of SciencesPolish Journal of Food and Nutrition Sciences2083-60072021-02-01711697710.31883/pjfns/133203133203Exploring the Interactions Between Caffeic Acid and Human Serum Albumin Using Spectroscopic and Molecular Docking TechniquesAli Jahanban-Esfahlan0Leila Roufegarinejad1Mahnaz Tabibiazar2José M. Lorenzo3Ryszard Amarowicz4Kidney Research Center, Tabriz University of Medical Sciences, Tabriz 5166-15731, IranDepartment of Food Sciences, Tabriz Branch, Islamic Azad University, Tabriz, IranDrug Applied Research Center, Tabriz University of Medical Sciences, Tabriz, IranCentro Tecnológico de la Carne de Galicia, Parque Tecnológico de Galicia, 32900 San Cibrao das Viñas, SpainDepartment 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, PolandUltraviolet-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 10 4 /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.http://journal.pan.olsztyn.pl/Exploring-the-Interactions-Between-Caffeic-Acid-and-Human-Serum-Albumin-Using-Spectroscopic,133203,0,2.htmlhuman serum albumin (hsa)fluorescencecaffeic acidinteractionmolecular docking |
| spellingShingle | Ali Jahanban-Esfahlan Leila Roufegarinejad Mahnaz Tabibiazar José M. Lorenzo Ryszard Amarowicz Exploring the Interactions Between Caffeic Acid and Human Serum Albumin Using Spectroscopic and Molecular Docking Techniques Polish Journal of Food and Nutrition Sciences human serum albumin (hsa) fluorescence caffeic acid interaction molecular docking |
| title | Exploring the Interactions Between Caffeic Acid and Human Serum Albumin Using Spectroscopic and Molecular Docking Techniques |
| title_full | Exploring the Interactions Between Caffeic Acid and Human Serum Albumin Using Spectroscopic and Molecular Docking Techniques |
| title_fullStr | Exploring the Interactions Between Caffeic Acid and Human Serum Albumin Using Spectroscopic and Molecular Docking Techniques |
| title_full_unstemmed | Exploring the Interactions Between Caffeic Acid and Human Serum Albumin Using Spectroscopic and Molecular Docking Techniques |
| title_short | Exploring the Interactions Between Caffeic Acid and Human Serum Albumin Using Spectroscopic and Molecular Docking Techniques |
| title_sort | exploring the interactions between caffeic acid and human serum albumin using spectroscopic and molecular docking techniques |
| topic | human serum albumin (hsa) fluorescence caffeic acid interaction molecular docking |
| url | http://journal.pan.olsztyn.pl/Exploring-the-Interactions-Between-Caffeic-Acid-and-Human-Serum-Albumin-Using-Spectroscopic,133203,0,2.html |
| work_keys_str_mv | AT alijahanbanesfahlan exploringtheinteractionsbetweencaffeicacidandhumanserumalbuminusingspectroscopicandmoleculardockingtechniques AT leilaroufegarinejad exploringtheinteractionsbetweencaffeicacidandhumanserumalbuminusingspectroscopicandmoleculardockingtechniques AT mahnaztabibiazar exploringtheinteractionsbetweencaffeicacidandhumanserumalbuminusingspectroscopicandmoleculardockingtechniques AT josemlorenzo exploringtheinteractionsbetweencaffeicacidandhumanserumalbuminusingspectroscopicandmoleculardockingtechniques AT ryszardamarowicz exploringtheinteractionsbetweencaffeicacidandhumanserumalbuminusingspectroscopicandmoleculardockingtechniques |