Blending effects on adsorption and micellization of different membrane protein solubilizers II. A thermodynamic study...

For a mixed system of a typical membrane protein solubilizer CHAPS (a derivative of a bile acid cholic acid) combined with a bile salt (sodium salt of glycocholic acid, NaGC), which is also a candidate as a membrane protein solubilizer, micellization and adsorbed film formation in a phosphate buffer solution of pH 7.4 at 303 K were studied paying special attention to the synergistic effect upon mixing. The collection of sufficient data based on plots of surface tension (gamma) versus logarithmic concentration (C(t) or m(t)) in total molality at discrete mole fractions (X(2)) in the mixture of surfactants 1 and 2 (where 1 and 2 correspond to CHAPS and NaGC, respectively) allowed us to accurately determine critical micelle concentration (CMC), minimum surface tension at CMC (gamma(CMC)), and the slope (dgamma/dlnC(t)) from the gamma-lnC(t) curves in the concentration range just below CMC. These data enabled us to estimate surface excess (Gamma(t)), and mean molecular area (A(m)) in addition to such parameters as the minimum surface Gibbs energy (G(min)((S))), pC(20) and CMC/C(20) related to synergism accompanied by blending. Applying the regular solution theory (RST), the relation of compositions of the singly dispersed phase (X(2)) and the micellar phase (Y(2)) as well as the interaction parameter (omega(R)) (by using the Rubingh's equations) were estimated. The relation between the composition in the adsorbed film (Z(2)) and X(2) together with the interaction parameter (omega(A)) in the adsorbed film was also estimated. The partial molecular area (PMA), gamma(CMC), and G(min)((S)) were examined as functions of X(2) and/or Z(2.) The resultant CMC-X(2) and CMC-Y(2) curves and omega(R) and omega(A) values have demonstrated that mixed micelles and adsorbed film formation are attained accompanying to some extent enhanced intermolecular interaction (with negative omega(R) and omega(A) values). Comparing with previous results for mixed systems of CHAPS with n-acyl (octanoly, nonanoyl, and decanoyl)-N-methylglucamides [MEGA-n's (n=8, 9, and 10)] and of sodium chenodeoxycholate (NaCDC) with sodium ursodeoxycholate (NaUDC), the synergism observed for the mixed system of CHAPS with NaGC lies between both combinations. However the expected properties as a membrane protein solubilizer are judged to be sufficient.