Adsorption of chemically radiolabeled [14C] collagen from binary mixtures with albumin or fibrinogen was studied on the solution/air and solution/polyethylene interfaces and revealed the preferential adsorption of albumin. This phenomenon is confirmed by the data of surface tension measurements of single protein, collagen-albumin, and collagen-fibrinogen solutions. Desorption experiments clearly show that more irreversibly adsorbed collagen was found on polyethylene surfaces when adsorption was performed from collagen-fibrinogen than from collagen-albumin solutions. The combined adsorption-desorption and the surface tension data show that competitive adsorption of collagen at the hydrophobic surfaces is strongly influenced by the surface tension properties of the proteins in solution.

We have studied self‐diffusion in DTAB micellar systems at three different salinities with fluorescence photobleaching experiments. In order to characterize interactions in these systems, we have also performed light scattering experiments. Despite of the strong variation of the interactions with salinities, almost no salinity variation in self‐diffusion coefficients vs droplets volume fraction curves has been observed. A clear difference between the friction coefficients involved in self‐ and mutual diffusion have been evidenced.

Collagen was isolated from rat tail tendons and acetylated with 1-14C acetic anhydride. In situ adsorption of this collagen from a buffer solution (pH = 2.7) was measured at the interfaces to air, polyethylene and polyethylene grafted with poly(maleic acid), respectively. The kinetics of adsorption were recorded for all surfaces studied and the corresponding diffusion coefficients for collagen in solution with various protein concentrations were calculated. The desorption of collagen from polymer surfaces was also studied. These experiments reveal the existence of both a reversibly and an irreversibly adsorbed collagen layer on the polymers tested. The desorption/adsorption ratio for the polyethylene is higher than that for the grafted polyethylene indicating stronger interactions of collagen with the grafted surface than with the non-modified polyethylene.

The insertion of myelin basic protein into microemulsion droplets of sodium bis (2-ethylhexyl) sulfosuccinate (AOT) has been studied by quasi-elastic light scattering. Measurements were made at both low and high molar ratios of water to surfactant, as a function of protein occupancy. The hydrodynamic radii of filled and empty droplets were experimentally evaluated. These were compared to values calculated using a water shell model of protein encapsulation, and excellent agreement was obtained. At low molar ratio of water to surfactant (w0 = 5.6), the hydrodynamic radius of filled droplets is significantly larger than the radius of empty ones. Under these conditions, about three empty (water-filled) droplets are required to build up a droplet of sufficient size to accommodate a single protein molecule. At maximum solubilization, which occurs at w0 = 5.6, a small fraction of droplets are found containing protein aggregates. In contrast, results at high values of w0 (22.4) reveal radii for empty and occupied droplets of comparable dimension, and the absence of aggregates. The results are discussed in terms of the model and the mechanism of interaction of this protein with the aqueous interfaces provided by these membrane-mimetic systems.

We report the first self-diffusion measurements of water-in-oil microemulsions done with fringe-pattern photobleaching-recovery techniques. These measurements give evidence of the onset of droplet aggregation which can be fairly distinct from the percolation threshold where an infinite aggregate is formed. Our results show that in some cases spherical droplets may not exist even at very low water-volume fractions. Above the observed onset, the self-diffusion coefficient reaches a nonzero limit value, reflecting the dynamical aspect of aggregation in these media.