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Molecular interactions of thymol with bovine serum albumin: Spectroscopic and molecular docking studies
Author(s) -
Roufegarinejad Leila,
JahanbanEsfahlan Ali,
SajedAmin Sanaz,
PanahiAzar Vahid,
Tabibiazar Mahnaz
Publication year - 2018
Publication title -
journal of molecular recognition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.401
H-Index - 79
eISSN - 1099-1352
pISSN - 0952-3499
DOI - 10.1002/jmr.2704
Subject(s) - thymol , chemistry , bovine serum albumin , quenching (fluorescence) , fluorescence spectroscopy , docking (animal) , enthalpy , hydrophobic effect , monoterpene , fluorescence , binding constant , chromatography , binding site , organic chemistry , biochemistry , thermodynamics , essential oil , medicine , physics , nursing , quantum mechanics
Thymol is the main monoterpene phenol present in the essential oils which is used in the food industry as flavoring and preservative agent. In this study, the interaction of thymol with the concentration range of 1 to 6 μM and bovine serum albumin (BSA) at fixed concentration of 1 μM was investigated by fluorescence, UV‐vis, and molecular docking methods under physiological‐like condition. Fluorescence experiments were performed at 5 different temperatures, and the results showed that the fluorescence quenching of BSA by thymol was because of a static quenching mechanism. The obtained binding parameters, K , were in the order of 10 4 M −1 , and the binding number, n, was approximately equal to unity indicating that there is 1 binding site for thymol on BSA. Calculated thermodynamic parameters for enthalpy (Δ H ), entropy (Δ S ), and Gibb's free energy (Δ G ) showed that the reaction was spontaneous and hydrophobic interactions were the main forces in the binding of thymol to BSA. The results of UV‐vis spectroscopy and Arrhenius' theory showed the complex formation in the interaction of thymol and BSA. Negligible conformational changes in BSA by thymol were observed in fluorescence experiments, and the same results were also obtained from UV‐vis studies. Results of molecular docking indicated that the subdomain IA of BSA was the binding site for thymol.