A spectroscopic and molecular dynamic approach on the interaction between ionic liquid type gemini surfactant and human serum albumin

Abstract

The interactions of imidazolium bashed ionic liquid-type cationic gemini surfactant ([C12-4-C12im]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-C12im]Br2 quenched the fluorescence of HSA through dynamic quenching mechanism as confirmed by time-resolved spectroscopy. The Stern-Volmer quenching constant (Ksv) and relevant thermodynamic parameters such as enthalpy change (ΔH), Gibbs free energy change (ΔG) and entropy change (ΔS) 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-C12im]Br2 with HSA induces conformational changes in HSA. Inquisitively, the molecular dynamics study contribute towards understanding the effect of binding of [C12-4-C12im]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.

Interaction of Indole Derivative with Human Serum Albumin: A Combined Spectroscopic and Molecular Dynamics Study

“…This faster diffusion of molecules increased the interaction between the fluorophore and quencher and thereby increased the quenching constant . These observations, indicated the presence of dynamic quenching mechanism . This was further confirmed by fluorescence lifetime measurements wherein decreased average lifetime of HSA was observed in the presence of ID (Table 4).…”

“…As one of the most abundant proteins in blood plasma, HSA performs multi‐functions in the body. Due to its extraordinary ligand‐binding capacity, it serves as a versatile transporter for many exogenous and endogenous ligands and drug molecules to their molecular targets ,. This globular soluble protein is synthesized and secreted from the liver.…”

Physicochemical study of biomolecular interactions between lysosomotropic surfactants and bovine serum albumin

“…mouthwash products and oral antiseptics). Their adverse effects can be avoided by the use of soft analogues of long-chain QACs, which are synthesized according to the soft drug approach and their physicochemi-as human serum albumin (HSA) [12] and bovine serum albumin (BSA) [13,14] can contribute towards a better understanding of the action of surfactants as solubilizing agents of membranes containing proteins and lipids [15]. BSA is commonly used as an expedient protein and is widely implicated as a general model to study the interactions of surfactants [14] and drugs [16] with globular proteins, not only due to its important roles in biological processes, but also because its structure is well established.…”

The role of chlorine atom on the binding between acrylonitrile derivatives and fat mass and obesity‐associated protein

“…The interaction between the derivative and FTO is static quenching. The binding constant K a and the number of binding sites ( n ) can be obtained from the double logarithmic Equation ) 49‐51 : …”