Chemometric studies of thymol binding with bovine serum albumin: A developing strategy for the successful investigation of pharmacological activity

• Published in: Bioelectrochemistry (Amsterdam, Netherlands) Netherlands), 2018-12, Vol.124, p.172-184
• Main Authors: Abbasi, Saleheh, Benvidi, Ali, Gharaghani, Sajjad, Rezaeinasab, Masoud
• Format: Article
• Language: English
• Subjects: Albumin binding study; Binding; Bovine serum albumin; Chemometric approaches; Differential pulse voltammetry; Docking; Electrochemistry; Essential oils; Hydrogen bonding; Hydrophobicity; Molecular docking; Pharmacology; Scientific imaging; Serum albumin; Spectroscopy; Thermodynamics; Thyme; Thymol; Van der Waals forces; Voltammetry
• ISSN: 1567-5394; 1878-562X
• DOI: 10.1016/j.bioelechem.2018.07.017

Thymol (Thy) is a hydrophobic active ingredient present in thyme essential oils. It is marginally soluble in water which is one of the challenging limitations for its application in foods or as drugs. An important aspect of our understanding from this system is to quantitatively comprehend how albumin interacts with Thy. Herein, this study has been focused on the interactions between thymol and bovine serum albumin (BSA) using electrochemical methods and ultraviolet and visible (UV–Vis) spectroscopy. Due to the overlap between obtained signals of existing species, it is apparent that multivariate methods can resolve overlapping signal trough unique decomposition. These obtained profiles are then analyzed to give the thermodynamic parameters, concentration and structural information of BSA binds to Thy. The thermodynamic results show that hydrogen bonding formation and van der Waals forces play major role in the binding process. Also, docking studies suggested that Thy binds mainly to the subdomain IIA of BSA through the formation of hydrogen bonding with Arg 217. Good agreement was found between the results obtained from experimental and theoretical studies. Thus, the current approaches seem to be promising that are not only for the transport of thymol in blood but also for its effective action in food applications. [Display omitted] •A strategy for increasing the solubility of thymol is use of protein delivery systems.•The interaction between thymol and BSA was investigated using voltammetric methods.•The best pose of thymol has ΔGbinding of −6.95 kJ mol−1 in the subdomain IIA.•According to the results of PARAFAC, complexes are formed with ratio of 1:4 and 1:2.•BSA-(Thy)6 is electroactive while BSA-(Thy)4 is not electroactive.