Probing the interaction of midazolam with human serum albumin: a biophysical investigation

• Published in: Journal of inclusion phenomena and macrocyclic chemistry Vol. 98; no. 3-4; pp. 197 - 204
• Main Authors: Ma, Xingang, Zhu, Yulin, Xie, Kun
• Format: Journal Article
• Language: English
• Published: Dordrecht Springer Netherlands 01.12.2020; Springer Nature B.V
• Subjects: Binding sites; Chemistry; Chemistry and Materials Science; Crystallography and Scattering Methods; Dichroism; Energy transfer; Fluorescence; Food Science; Hydrogen bonding; Organic Chemistry; Original Article; Serum albumin; Human serum albumin; Interaction mechanism; Spectroscopy; Midazolam
• ISSN: 1388-3127; 1573-1111
• DOI: 10.1007/s10847-020-01016-8

Herein, the spectroscopic methods were applied for investigating the interaction between human serum albumin (HSA) and midazolam in simulated physiological environments. The fluorescence quenching of HSA by midazolam followed the static mode. The association constant at 293 K was obtained as 1.73 × 10 4  M −1 with probably one binding site between midazolam and HSA. The results of thermodynamic parameters revealed that the hydrogen bonding was the dominating force in the interaction. The results of UV–Vis spectra, synchronous fluorescence, and circular dichroism results showed that binding with midazolam subtly changed the HSA’s conformation along with the secondary structure. The results of Förster resonance energy transfer showed a possible 3.48 nm energy transfer distance with Trp-214 to midazolam. This study aimed to provide valuable information for further research on pharmacological mechanisms and the toxicological and distribution of midazolam in vivo.