Protocol for evaluating drug-protein interactions based on fluorescence spectroscopy.

Investigating the interactions between ligands, such as drugs, and proteins is essential to understand their functions and effects. This fluorescence spectroscopy protocol details how to analyze the effects of drugs on protein structure, including steps for solution preparation, fluorescence spectra collection, and results analysis. It is applicable to studying drug-protein interactions, binding affinity, and thermodynamic parameters as well as performing further studies on drug design.

Mechanistic insights into the interaction of anxiolytic drugs with human serum albumin in a ternary system utilizing spectroscopic and molecular modeling approaches.

In recent years, buspirone has been co-administered with sertraline to resolve sexual disorders caused by sertraline. Therefore, the present study was conducted to investigate the interaction effect of two antidepressants and anxiolytic drugs, sertraline and buspirone, on human serum albumin (HSA) using spectroscopic and molecular docking techniques. Fluorescence emission spectroscopy and molecular docking were used to calculate the binding affinity and determine the best binding sites for these two drugs.

Insights into the binding of buspirone to human serum albumin using multi-spectroscopic and molecular docking techniques.

Buspirone is an anxiolytic drug that plays a significant role in managing anxiety disorders and alleviating their symptoms as well. Several techniques were utilized to study the interaction between buspirone and human serum albumin under physiological conditions, including UV-vis absorption spectroscopy, fluorescence emission spectroscopy, circular dichroism, Fourier transform infrared spectroscopy (FT-IR), equilibrium dialysis, and molecular docking. The results of this study demonstrated that buspirone quenched the intrinsic fluorescence of human serum albumin through a mixed mechanism.