Multianalytical and Theoretical Tendency for the Clarification of the Binding of Lansoprazole and Albumin Protein

) values. UV-vis absorption spectroscopy confirmed structural changes in BSA upon LAN binding, while three-dimensional fluorescence spectroscopy showed changes in the microenvironment of tryptophan and tyrosine residues. Electrochemical studies also supported the formation of a stable, nonelectroactive LAN-BSA complex, leading to decreased peak currents. Molecular docking and molecular dynamics simulations provided atomic-level information, showing that LAN preferentially binds to the I site of BSA, stabilized by hydrogen bonding and hydrophobic interactions. Circular dichroism spectral results indicated a secondary structural change in HSA upon LAN binding. The findings of this study contribute to a better understanding of the pharmacokinetic behavior of LAN, providing valuable information about its therapeutic efficacy and potential drug-protein interactions.