Biophysical analysis of a novel oxy-diester hybrid cationic gemini surfactants (Cm-E2O-Cm) with xanthine oxidase (XO)
Mohd. Akram, Imtiyaz Ahmad Bhat, Sana Anwar, Kabir-ud-Din
Surfactant ̶ protein/enzyme interactions have gained widespread interest in modern research due to their implications in various domains like pharmaceuticals, cosmetics or biotechnology. Thus, spectroscopic, microscopic and molecular modeling approaches have been employed to explore the interaction of a novel series of oxy-diester hybrid cationic gemini surfactants; 2,2’-[(oxybis(ethane-1,2-diyl))bis(oxy)]bis(N-alkyl-N,N-dimethyl-2- 3 oxoethanaminium) dichloride (C12-E2O-C12, C14-E2O-C14 and C16-E2O-C16) with bovine milk xanthine oxidase (XO). Fluorescence studies revealed that concerned gemini surfactants quenched the XO fluorescence through a static quenching mechanism. The trend for Ksv values was: C12-E2O-C12 < C14-E2O-C14 < C16-E2O-C16 while the inverse trend was observed for Kb values (C12-E2O-C12 > C14-E2O-C14 > C16-E2O-C16). Negative o ΔGb values confirmed the spontaneity of Cm-E2O-Cm + XO interactions. The results of other techniques (like pyrene fluorescence, UV, CD and TEM) also indicated that the concerned gemini surfactants induce conformational changes in XO. Moreover, the actual binding site of Cm-E2O-Cm gemini surfactants into hydrophobic domains of XO was confirmed by molecular docking. This study elucidates the interaction mechanism of high performance gemini surfactants with proteins/enzymes, which may be significant to compile the green amphiphilic systems, for industrial and pharmaceutical implications (more specifically to develop chemical entities for prevention and treatment of various diseases like gout, hyperuricemia, etc.).
Circular dichroism, Secondary structure, Ligand binding, Biochemistry