Research Article

In Vitro Characterization of the Interactions of Human Serum Albumin with Rosuvastatin and Atorvastatin Using Fluorescence Spectroscopy and Molecular Modeling

Aida Smajlović
University of Tuzla, Bosnia and Herzegovina
Alen Hatkić
University of Tuzla, Bosnia and Herzegovina
Esmeralda Dautović
University of Tuzla, Bosnia and Herzegovina
* Corresponding author
Daria Pavlić
Pharmacy Ibn Sina, Bosnia and Herzegovina
Adaleta Softić
University of Tuzla, Bosnia and Herzegovina
Nahida Srabović
University of Tuzla, Bosnia and Herzegovina
Dalila Halilčević
University of Tuzla, Bosnia and Herzegovina
Asja Šarić
University of Tuzla, Bosnia and Herzegovina
DOI icon 10.24018/ejchem.2023.4.4.145

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Submitted 2023-07-17
Published 2023-10-18

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Article Main Content

Human serum albumin (HSA) is one of the most important transporters for drugs in the systemic circulation. In this study, we investigated the interaction of rosuvastatin (ROS) and atorvastatin (ATO) with HSA. Binding of a drug molecule to HSA significantly affects the pharmacokinetics of the drug as it increases drug solubility in plasma, decreases toxicity and protects molecules from oxidation. This study was made using fluorescence spectroscopy and molecular modeling approach. Fluorescence spectra were recorded for two different statins brands at seven different concentrations. The results revealed that both statins (ROS and ATO) cause the fluorescence quenching of the HSA solution. ROS and ATO binds strongly to HSA with the binding constant (Kb) of 1.0246×106 and 0,9018×106, respectively. In addition, it was observed that high concentrations of ATO cause a shift of the emission maximum towards longer wavelengths (red-shift), which may be due to the unfolding of protein chains or denaturation. Furthermore, it was calculated that HSA possesses one binding site for ROS and ATO. Results from molecular docking showed that ROS has a higher affinity for Sudlow site I compared to Sudlow site II and the main binding forces are hydrogen bonds. ATO has nearly equal affinity for both binding sites on HSA, and the main binding forces are hydrophobic interactions.

Keywords: Atorvastatin Fluorescence quenching Human serum albumin Rosuvastatin

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