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.

百里香酚（Thymol）是百里香精油中的一种疏水性活性成分。它微溶于水，这是其在食品或药物中应用的挑战性限制之一。我们从该系统了解的一个重要方面是定量理解白蛋白如何与Thy相互作用。在这里，这项研究集中在百里酚和牛血清白蛋白（BSA）之间的相互作用，采用电化学方法以及紫外和可见（UV-Vis）光谱法。由于现有物种获得的信号之间存在重叠，因此很明显，多变量方法可以解决重叠信号通过唯一分解的问题。然后分析这些获得的概况，以给出与Thy结合的BSA的热力学参数，浓度和结构信息。热力学结果表明，氢键的形成和范德华力在结合过程中起主要作用。此外，对接研究表明，Thy通过与Arg 217形成氢键而主要结合BSA的IIA亚结构域。从实验研究和理论研究得出的结果之间发现了很好的一致性。因此，当前的方法似乎是有前途的，不仅用于在血液中运输百里香酚，而且还用于其在食品应用中的有效作用。