Interaction of remimazolam benzenesulfonate and human serum albumin: a simulated physiological study.

Herein, to elucidate the interaction mechanism and physicochemical properties of remimazolam and human serum albumin (HSA) interactions, techniques such as fluorescence, circular dichroism (CD) spectroscopy and isothermal titration calorimetry have been applied for study. The thermodynamic parameters at body temperature (ΔS=-207 J·mol-1 ·K-1 , ΔS=-9.76×104 J·mol-1 and ΔG=-3.34×104 J·mol-1 ; 310 K) manifests one strong binding site on the protein, which was modulated by van der Waals forces and hydrogen bonds. What is more, the results of CD, synchronous and three-dimensional fluorescence manifested that remimazolam altered the microenvironment of the protein amino acid residues. A distance of 2.1 nm between the remimazolam and Trp shows potential of resonance energy transfer. Furthermore, these results potentially provide information for illustrating the pharmacodynamics and toxicodynamics of remimazolam when it is applied clinically.