Binding Interaction Characterization between Antimalarial Artemisinin (Art) and Bovine Serum Albumin (BSA) Using Fluorescence Emission Spectroscopy

Artemisinin (ART) has been widely used as antimalarial drug for the treatment of multiple drug-resistant strains of plasmodium falciparum. In this resarch, the binding interaction of ART with bovine serum albumin (BSA) under the limited physiological conditions (pH 7.4) was conductedusing fluorescence emission spectroscopy. The results revealed that there was a static quenching of BSA induced by ART due to the formation of ART–BSA complex. The binding constants and number of binding sites of ART with BSA under simulated physiological condition (pH=7.4) were -0.61 and 2.5 at 288 K, -2.81 and 2.0 at 298 K, -3.21 and 1.8 at 300 K respectively. Based on the signs and magnitude of the enthalpy and entropy changes, it could be suggested that the binding process of ART and BSA was spontaneous and the main interaction forces of ART with BSA were van der Waal’s forces and hydrogen bonding interactions.