Spectrometric, Thermodynamic, pH Metric and Viscometric Studies on the Binding of TEALS as Surfactant with Albumin as Biopolymer

摘要

Background: Since the interactions of small anions with protein are very importantin their transportation and distribution processes in biological systems, it is helpfulto study these interactions to understand the nature of the transportation and distributionprocesses. Therefore, it is aimed to study the interaction of albumin with surfactant moleculeby different physical methods.Objective: Present work attempts to work on assessing the structure, characterization of thesurfactants as TEALS (tri-ethanalamine lauryl sulphate) binding sites, with albumin involvedin various process of living being are discussed.Methods: The binding of surfactant TEALS to egg protein has been studied at different pHvalues and temperatures by spectrophotometric and equilibrium dialysis methods. Thebinding data were found to be pH and temperature dependent. The binding data studied bythe absorbance method, were found approximately identical with those obtained from theequilibrium dialysis method.Results: The association constants and the number of binding sites were calculated fromScatchard plots and found to be at maximum at lower pH and at lower temperature. Thefree energy of the combining sites was lowest at higher pH and highest at low pH. Therefore,a lower temperature and a lower pH offered more sites in the protein molecule for interactionwith surfactant. The ΔG (free energies of aggregation) associated with the bindinginteraction of the surfactants and protein were calculated. The negative values of theΔG confirm the feasibility of interaction between the surfactant and protein. All the observationsrecorded in this paper indicate that the TEALS has a good affinity of binding withegg protein and the number of binding sites is dependent on various physical and chemicalfactors.Conclusion: On the basis of the results of the experiments which were conducted to examinethe interaction between anionic surfactant and protein by measuring the various parametersof the solutions, it is concluded that the interaction of surfactant and protein gives anidea of fundamental understanding of the structure of surfactant-protein complex and theirpractical applications in every field.