화학공학소재연구정보센터
Langmuir, Vol.23, No.2, 771-775, 2007
Lack of association between a cationic protein and a cationic fluorosurfactant
Surface tension, F-19 and H-1 NMR spectroscopy, and cryotransmission electron microscopy are used to characterize the state of association in aqueous solutions of a fluorosurfactant CF3(CF2)(n)SO2NH(CH2)(3-4)N(CH3)(3)(+) I- (n = 8, 6) with and without lysozyme added. In the absence of lysozyme, we find monomers, small aggregates, and large vesicles to coexist, with the individual fluorosurfactant molecules exchanging slowly (> 1 ms) among those states. When both lysozyme and fluorosurfactant are present in the solution, they have no measurable influence on the physical state of the other. In contrast, a hydrogenated cationic surfactant with the same headgroup, hexadecyltrimethylammonium bromide, is shown to associate to lysozyme.