Blending effects on adsorption and micellization of different membrane protein solubilizers: A thermodynamic study on three mixed systems of CHAPS with MEGA-8, -9 and -10 in pH 7.2 phosphate buffer solution

Abstract

By means of surface tension measurement (Wilhelmy method), micellization and adsorbed film formation were investigated for three combinations of mixed surfactant systems, all of which are used for solubilizing membrane proteins: a typical zwitterionic surfactant, CHAPS (a derivative of cholic acid) with n-alkyl (octyl, nonyl and decyl)- N-glucamides, MEGA- n ( n = 8, 9, 10). The data based on plotting of surface tension ( γ) versus logarithmic total molarity (or molality) ( C t or M t) as a function of mole fraction of surfactant 2 (2 corresponds to MEGA- n's) enabled us to determine critical micellization concentration (CMC), minimum surface tension at CMC ( γ CMC), surface excess ( Γ t), mean molecular surface area ( A m), the minimum Gibbs energy ( G min ( S ) ) of adsorbed film of both single and mixed surfactant systems and partial molecular area (PMA) in addition to parameters such as p C 20 and CMC/ C 20 being related to synergism accompanied by blending (mixing) in regard to surface activity as well as micelle forming ability. On the basis of the regular solution theory, the relations of compositions of singly dispersed phase ( X 2), micellar phase ( Y 2) and adsorbed film ( Z 2) were estimated, and then the interaction parameters in micelles ( ω R) and in the adsorbed film phase ( ω A) were also calculated. From both the CMC– X 2 and CMC– Y 2 curves, it was found for all the combinations to show synergistically enhanced ability of mixed micelle formation as well as surface tension reduction. The resultant synergism coming from blending CHAPS with MEGA- n's was discussed in comparison with different combinations of various types of surfactants including membrane proteins solubilizers.