Probing amikacin interaction with albumin: A combined multispectral and molecular docking investigation

The fate of a drug administered to a living organism depends on the pharmacological and pharmacokinetic behavior of drugs. Biological macromolecules like serum albumins have a crucial role in the design and biological safety assessments of drugs. Amikacin as an example of the most used semi-synthetic aminoglycosides antibiotics, is included in the crucial drug list of the World Health Organization. This in vitro study aimed to explore Amikacin's binding specification with bovine serum albumin (BSA) through a computational and experimental approach. According to fluorescence spectra, it was declared that the innate fluorescence emission of serum albumin was quenched by the Amikacin via a static quenching mechanism. Meantime, the binding constants and thermodynamic parameters of Amikacin with BSA were calculated at various temperatures. Based on this calculation, negative Δ<i>G</i>°, Δ<i>H</i>°, and Δ<i>S</i>° values showed that spontaneous binding process occurred via hydrogen bond and van der Waals interaction. Additionally, based on UV-vis absorption, Amikacin leads to conformational modifications of BSA with the construction of a ground state complex, which may affect the physiological functions of this serum albumin. The results of FTIR spectroscopy showed that the binding of amikacin led in the change of BSA secondary structure and confirmed the possibility of changing the physiological functions of BSA. It is anticipated that this research will supply significant insight into the pharmacological properties of Amikacin and its related effects on human health <i>in vivo</i>.