Abstract
Binding effect and interaction of N,N'-dialkyl cystine based gemini surfactant (GS); 2(C(12)Cys) with human serum albumin (HSA) were systematically investigated by the techniques such as surface tension measurement, UV-visible spectroscopy, fluorescence spectroscopy, circular dichroism (CD) spectroscopy, and molecular docking studies. The surface tension measurement exhibited that HSA shifted the critical micelle concentration of the 2(C(12)Cys) GS to the higher side that confirms the complex formation among 2(C(12)Cys) GS and HSA which was also verified by UV- visible, fluorescence, and CD spectroscopy. Increase in the concentration of 2(C(12)Cys) GS increases the absorption of the HSA protein but has a reverse effect on the fluorescence intensity. The analysis of UV-visible study with the help of a static quenching method showed that the value acquired for the bimolecular quenching constant (k(q)) quenches the intrinsic fluorescence of the HSA protein. Synchronous fluorescence spectrometry declared that the induced-binding conformational changes in HSA and CD results explained the variations in the secondary arrangement of the protein in presence of 2(C(12)Cys) GS. The present study revealed that the interaction between 2(C(12)Cys) GS and HSA is important for the preparation and properties of medicines. Molecular docking study provides insight into the specific binding site of 2(C(12)Cys) GS into the sites of HSA.