A spectroscopic and molecular dynamic approach on the interaction between ionic liquid type gemini surfactant and human serum albumin. Issue 10 (2nd October 2016)

• Record Type: Journal Article
• Authors: Maurya, Jitendra Kumar; Mir, Muzaffar Ul Hassan; Maurya, Neha; Dohare, Neeraj; Ali, Anwar; Patel, Rajan
• Is Part Of: Journal of biomolecular structure & dynamics. Volume 34:Issue 10(2016)
• Page Start: 2130
• Page End: 2145
• Publication Date: 2016-10-02
• Subjects: gemini surfactant -- HSA -- quenching -- hydrophobic interaction -- molecular dynamics; Biomolecules -- Periodicals; Molecular structure -- Periodicals; Molecular Biology -- Periodicals; Biomechanics -- Periodicals; 572
• DOI: 10.1080/07391102.2015.1109552
• Languages: English
• ISSNs: 0739-1102

Abstract

Abstract : The interactions of imidazolium bashed ionic liquid-type cationic gemini surfactant ([C12 -4-C12 im]Br2 ) with HSA were studied by fluorescence, time-resolved fluorescence, UV-visible, circular dichroism, molecular docking and molecular dynamic simulation methods. The results showed that the [C12 -4-C12 im]Br2 quenched the fluorescence of HSA through dynamic quenching mechanism as confirmed by time-resolved spectroscopy. The Stern–Volmer quenching constant ( K sv ) and relevant thermodynamic parameters such as enthalpy change (Δ H ), Gibbs free energy change (Δ G ) and entropy change (Δ S ) for interaction system were calculated at different temperatures. The results revealed that hydrophobic forces played a major role in the interactions process. The results of synchronous fluorescence, UV-visible and CD spectra demonstrated that the binding of [C12 -4-C12 im]Br2 with HSA induces conformational changes in HSA. Inquisitively, the molecular dynamics study contribute towards understanding the effect of binding of [C12 -4-C12 im]Br2 on HSA to interpret the conformational change in HSA upon binding in aqueous solution. Moreover, the molecular modelling results show the possible binding sites in the interaction system.