Non-ionic surfactants in drug delivery vehicles: Physicochemical insights with systems of drugs, Igepal CA-630, bovine serum albumin and hen egg-white lysozyme

Molecular Interactions between a Flavonoid and Lysozyme: A Spectroscopic, Thermodynamic, and Computational Study

“…Here the equilibrium attains in this interaction by leading hydrophobic forces along and over the other forces like hydrogen boning breaking and formation due to the rearrangement of water molecules. [41,42] Here solvent water molecule near the hydrophobic part of LYZ & hydrophilic part of LYZ itself getting rearrangement in phosphate buffer at pH 7.4 and this is a wellknown fact that the water molecule plays an important role in PÀ L interactions to form & sustain the protein-ligand complex. This is a phenomenon for most of the PÀ L interaction in water buffer which governs the reaction and post-complexed protein structure, in the study, the change of entropic effect so obtained from ITC data see Table 1, is ΔS 65.0 Cal Mol À 1 this is the lower in magnitude than a change of enthalpy indicates the PÀ L complexation as the extent of solvation effect of protein in the cell which is very low and the degree of freedom of the system reached a small value which indicates the stability of PÀ L complex, also here the enthalpy contribution leads the interaction as enthalpy driven reaction.…”