Study on the binding of sulfaclozine sodium monohydrate with bovine and human serum albumins using multi-spectroscopy and molecular docking

The interactions of sulfaclozine sodium monohydrate (SSM) with bovine and human serum albumins (BSA and HSA) were studied by multi-spectroscopy and molecular docking technique. Stern-Volmer analysis and fluorescence lifetime measurements suggested the quenching processes were static. According to the Fluorescence resonance energy transfer (FRET) theory, the binding distances were obtained indicating SSM interacted with BSA/HSA along with non-radiation energy conversion. Electrostatic attraction was the main force in keeping the stability of the compound based on thermodynamic parameters. Circular dichroism (CD), synchronous fluorescence and Fourier Transform infrared (FT-IR) spectra embodied the secondary structures of serum albumins were transformed by SSM. The site marker competitive and molecular docking measurements testified SSM bound to BSA/HSA at site I. In conclusion, the secondary structures of BSA/HSA were changed by SSM in the static fluorescence quenching processes with the non-radiation energy conversion. The binding sites were all located at site I and electrostatic attraction was the main force for the new compound. Communicated by Ramaswamy H. Sarma

Automated summary

The study investigated the interactions of sulfaclozine sodium monohydrate with bovine and human serum albumins using multi-spectroscopy and molecular docking techniques. The main force maintaining the stability of the compound was found to be electrostatic attraction based on thermodynamic parameters. Results from fluorescence measurements and molecular docking showed that SSM interacted with BSA/HSA predominantly at site I.