Design and characterization of BSA-mycophenolic acid nanocomplexes: Antiviral activity exploration

Abstract

The interactions between bovine serum albumin (BSA) and mycophenolic acid (MPA) were investigated in silicothrough molecular docking and in vitro, using fluorescence spectroscopy. Dynamic light scattering and scanningelectron microscopy were used to figure out the structure of MPA-Complex (MPA-C). The binding affinity betweenMPA and BSA was determined, yielding a Kd value of (12.0 ± 0.7) μM, and establishing a distance of 17 Åbetween the BSA and MPA molecules. The presence of MPA prompted protein aggregation, leading to the formationof MPA-C. The cytotoxicity of MPA-C and its ability to fight Junín virus (JUNV) were tested in A549 andVero cell lines. It was found that treating infected cells with MPA-C decreased the JUNV yield and was moreeffective than free MPA in both cell line models for prolonged time treatments. Our results represent the firstreport of the antiviral activity of this type of BSA-MPA complex against JUNV, as assessed in cell culture model systems. MPA-C shows promise as a candidate for drug formulation against human pathogenic arenaviruses.