Ankara Universitesi Eczacilik Fakultesi Dergisi, cilt.49, sa.3, ss.859-869, 2025 (Scopus, TRDizin)
Objective: This research investigated the interaction between Eltrombopag (EB) and Human Serum Albumin (HSA) by fluorescence spectroscopy and voltammetry while explaining the quenching mechanism. Material and Method: The electrochemical studies were conducted in an acetate buffer solution (AB) at pH 4 by differential pulse voltammetry (DPV). For the fluorescence studies, EB, HSA, and a mixture of EB and HSA solutions were designed with a pH of 4.7, AB containing 20% DMSO. Result and Discussion: The interaction between EB and HSA was examined by fluorescence and electrochemical titrations, which showed a quenching effect and peak shifting. Fluorescence titrations indicate that EB’s HSA quenching process is static and has a hypsochromic shift. Analysis of thermodynamic parameters and higher binding constants concluded a strong and spontaneous interaction. Electrochemical titrations show the intercalation of EB into HSA.