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Abstract
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The serum albumins are the most abundant members of the albumin family of globular protein. Albumin has the characteristics of an acidic, highly soluble, and highly stable protein that can endure 60°C for 10 hours. This protein regulates 80% of osmotic blood pressure, pH of the blood and circulates 28 times in the lymphatic system during its lifetime, having a substantial impact on drug delivery and efficiency, as well as providing pharmacokinetic data (absorption, distribution, metabolism, and excretion of drugs). The ligand used in this investigation is remdesivir, an adenosine analog pro-drug that inhibits Covid-19 replication by inhibiting virus RNA synthesis. Absorption spectroscopy and fluorescence methods were used to explore the structural alterations of human serum albumin (HSA) in the presence of various concentrations of remdesivir and the effect of environmental conditions such as temperature (25 to 37 ºC) and drug concentration (0.5 to 5 µM) on the interaction of albumin and drug. Examinations have shown that the absorption intensity of HSA expanded with the increase of drug concentration, and the fluorescence emission decreased due to the quenching process. Using quenching data, first, Stern-Volmer constant (Ksv) was obtained. Then, the binding constant (Kb) and the number of binding sites (n) were calculated using the Stern-Volmer diagram. According to the results obtained from the quenching phenomenon, remdesivir drug binds to HSA by a static mechanism with a binding site number of around 1. Also, the spontaneity of the interaction was explored using the Van't Hoff equation, which indicated the self spontaneity of the interaction between HSA and the drug. As a result, the remdesivir drug can bind to HSA spontaneously and trigger some conformational changes in the protein due the its carrier to the target.
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