Energetics of the interactions of human serum albumin with cationic surfactant

Surface active ionic liquids: Study of the micellar properties of 1-(1-alkyl)-3-methylimidazolium chlorides and comparison with structurally related surfactants

“…The only member of the C n PyCl series that has been studied in detail is C 16 PyCl [16,[24][25][26][27][28][29][30][31][32][33][34][35][36]. As can be seen from the data of Table SM-3, the other members have not received much attention.…”

Micellar properties of surface active ionic liquids: A comparison of 1-hexadecyl-3-methylimidazolium chloride with structurally related cationic surfactants

“…The dependence of E obs T on the mole fraction of water, v W , is known for QBS in the above mentioned binary mixtures, Eqs. (18) and (19) [76,77]. The values of v W were converted into molarity of interfacial water from the weights of the two component solvents, and density of the binary mixture.…”

“…Although the micellar properties of C 16 PyCl have been studied by several authors [9][10][11][12][13][14][15][16][17][18][19][20][21], none has covered the temperature range employed in the present study (15-75°C). More importantly, however, there are problems associated with the calculation of the degree of counter-ion dissociation, a mic ; the enthalpy of micellization, DH mic , or both, vide infra and The concentration of water in the interfacial regions has been calculated by employing an anionic solvatochromic indicator, 1-methylquinolinium-8-olate-5-sulfonate, QBS, Chart 2; the values were found to be 42.2 ± 2 and 38.5 ± 2 mol L À1 , depending on the binary solvent mixture that is used as a reference for interfacial water.…”

Binding of streptomycin with bovine serum albumin: Energetics and conformational aspects

“…Though the interactions of some antibiotics with the serum albumin are reported in literature [11,[17][18][19], quantitative studies on the interaction of streptomycin with serum albumin addressing the energetics and type of interactions is not available in literature. A combination of isothermal titration calorimetry and fluorescence spectroscopy has yielded valuable information on binding interactions in biologically important systems both quantitatively and qualitatively [20][21][22][23][24][25]. In this work, we have used isothermal titration calorimetry in determining binding affinity, enthalpy, entropy and stoichometry …”