Molecular Interaction of Amino Acid-Based Gemini Surfactant with Human Serum Albumin: Tensiometric, Spectroscopic, and Molecular Docking Study

Jeenat Aslam; Irfan Hussain Lone; Nagi R E Radwan; Mohd Faizan Siddiqui; Shazia Parveen; Rua B Alnoman; Ruby Aslam

doi:10.1021/acsomega.9b03315

Molecular Interaction of Amino Acid-Based Gemini Surfactant with Human Serum Albumin: Tensiometric, Spectroscopic, and Molecular Docking Study

ACS Omega. 2019 Dec 9;4(26):22152-22160. doi: 10.1021/acsomega.9b03315. eCollection 2019 Dec 24.

Authors

Jeenat Aslam¹, Irfan Hussain Lone¹, Nagi R E Radwan¹, Mohd Faizan Siddiqui², Shazia Parveen¹, Rua B Alnoman¹, Ruby Aslam³

Affiliations

¹ Department of Chemistry, College of Science, Taibah University, Yanbu 30799, Saudi Arabia.
² Department of Biochemistry, Aligarh Muslim University, Aligarh 202002, India.
³ Corrosion Research Laboratory, Department of Applied Chemistry, Faculty of Engineering and Technology, Aligarh Muslim University, Aligarh 202002, India.

Abstract

Binding effect and interaction of N,N'-dialkyl cystine based gemini surfactant (GS); 2(C₁₂Cys) 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(C₁₂Cys) GS to the higher side that confirms the complex formation among 2(C₁₂Cys) GS and HSA which was also verified by UV-visible, fluorescence, and CD spectroscopy. Increase in the concentration of 2(C₁₂Cys) 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(C₁₂Cys) GS. The present study revealed that the interaction between 2(C₁₂Cys) GS and HSA is important for the preparation and properties of medicines. Molecular docking study provides insight into the specific binding site of 2(C₁₂Cys) GS into the sites of HSA.