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

Aida Smajlović, Alen Hatkić, Esmeralda Dautović, Daria Pavlić, Adaleta Softić, Nahida Srabović, Dalila Halilčević and Asja Šarić
Additional contact information
Aida Smajlović: University of Tuzla, Bosnia and Herzegovina
Alen Hatkić: University of Tuzla, Bosnia and Herzegovina
Esmeralda Dautović: University of Tuzla, Bosnia and Herzegovina
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

European Journal of Advanced Chemistry Research, 2023, vol. 4, issue 4, 9-15

Abstract: 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 (search for similar items in EconPapers)
Date: 2023
References: Add references at CitEc
Citations:

Downloads: (external link)
https://eu-opensci.org/index.php/ejchem/article/view/5145 Abstract page (text/html)
https://eu-opensci.org/index.php/ejchem/article/download/5145/1260 Full text (application/pdf)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:epw:ejchem:v:4:y:2023:i:4:id:5145

DOI: 10.24018/ejchem.2023.4.4.145

Access Statistics for this article

More articles in European Journal of Advanced Chemistry Research from European Open Science
Bibliographic data for series maintained by Support Team ().