Interaction of of human serum albumin with diclofenac incorporated in catanionic vesicles

In this study, we have prepared a cationic SDS/CTAB vesicle membrane and a non-steroidal anti-inflammatory (NSAID) drug, diclofenac sodium was incorporated in it. Further, the interaction of human serum albumin with diclofenac and diclofenac incorporated cationic vesicle was studied by different techniques such as, scanning electron microscopy (SEM), dynamic light scattering (DLS), FTIR, UV-visible and fluorescence spectroscopy. The dynamic light scattering interprets that the particle size of the HSA-vesicle system is greater as related to their pure vesicle system. The CD data clearly suggests that cationic vesicles do not have any denaturising effect on HSA (human serum albumin). The fluorescence results show the strong quenching with the formation of complex between HSA and diclofenac vesicle with static quenching. The binding constant, Kb of HSA with DIC incorporated catanionic vesicle is less than the binding constant of HSA-DIC interaction, this shows the slow release of drug from the vesicle. The UV-visible results suggest that DIC in presence of vesicles connects with HSA and shows no apparent effect on the micro-environment of the fluorophore residues of HSA. (C) 2019 Elsevier Ltd. All rights reserved.