Multi-spectroscopic and theoretical analysis on the interaction between human serum albumin and Cm-E2O2-Cm gemini surfactants

Abstract

Human serum albumin (HSA) is among the blood plasma proteins crucial for transporting various natural and pharmaceutical substances throughout the body. This research examined how the structure of HSA changes when exposed to Cm-E2O2-Cm gemini surfactants, which possess various advantageous properties, utilizing a combination of multispectral analysis and computational modeling techniques. The aggregation behavior of gemini surfactants in the presence of HSA was also investigated to demonstrate the HSA-Cm-E2O2-Cm complexation. The intrinsic fluorescence findings showed that gemini surfactants caused HSA fluorescence to diminish due to static quenching. The binding constants (Kb) for HSA-Cm-E2O2-Cm at varying temperatures were around 103 M−1, with approximately one binding site detected. In addition, the effect of gemini surfactants on the conformation of HSA was analyzed by performing UV–vis, extrinsic, synchronous, RRS and 3-D fluorescence, and CD experiments. The interactions’ binding sites and driving forces (also spontaneity) were calculated using molecular docking analysis, which agrees with site marker studies and thermodynamic parameter value results.