ABSTRACT
Dilute mixtures of the water soluble polymer polyethyleneimine (PEI) and the cationic surfactant cetyltrimethylammonium bromide (CTAB) form mesostructured thin films at the air/solution interface. In this paper we show that these films form spontaneously, reaching an equilibrium composition. When the film is removed, a new solid film rapidly reforms, with a similar morphology when inspected by Brewster angle microscopy (BAM). Successive removal of films lead to a series of structurally similar films, until the amount of surfactant in solution approaches the lower limit of film forming concentration. The results obtained using surfactant-selective potentiometry suggest that the incipient polymer:surfactant aggregates are in a position to migrate to the surface rapidly after film removal, prior to mesostructure formation. X-ray reflectivity indicates that films formed at different PEI:CTAB compositions retain mesophase regular structures with the same d-spacing feature, equal to 52.2A. Grazing incidence diffraction measurements indicate that films are composed of small crystallites arranged in a random powder fashion, developing a rough surface morphology evidenced by BAM. The central finding is that PEI:CTAB films form when the amount of CTAB in solution is higher than a critical film formation concentration, very close to the critical aggregation concentration (CAC), allowing the formation of several equilibrated films from the same growing solution.
ABSTRACT
The effect of the addition of short-chain monohydric alcohols (ethanol and propan-2-ol) to the protein:surfactant system lysozyme:sodium dodecyl sulfate (Lz:SDS) in aqueous solution was investigated using a conductometric technique. A second protein:surfactant system, bovine serum albumin:SDS (BSA:SDS) was also investigated so that the effect of a different protein conformation and composition could be compared. The critical aggregation concentration (CAC) of the protein forming the complex and the critical micelle concentration (CMC *) of SDS in the presence of protein, at different alcohol concentrations, were determined. It was found in both cases that the addition of alcohol does not produce a significant change in the CAC, whereas the CMC * displays variation with alcohol concentration that shows an inversion in the ranges 0.05-0.06 ethanol mole fraction and 0.02-0.03 propan-2-ol mole fraction. This suggests that, in contrast with the CAC behaviour, the major factor that drives SDS micellization in the presence of protein is the variation in water structure. Results also suggest that it occurs in the same way for both proteins, where electrostatic interactions are the main force in the formation of the complex. Conversely, hydrophobic interactions play the dominant role at the micellization stage, and only the extent of the interaction between protein:surfactant aggregates and surfactant species seems to depend on protein nature.
