The Elutability of Fibrinogen by Sodium Dodecyl Sulphate and Akyltrimethylammonium Bromides.

The elutability of adsorbed fibrinogen by cationic surfactants of different chain lengths (dodecyltrimethylammonium bromide, tetradecyltrimethylammonium bromide, cetyltrimethylammonium bromide), and an anionic surfactant (sodium dodecyl sulphate (SDS)) was studied using in situ ellipsometry. The concentrations of the surfactants were twice the CMC in water and for fibrinogen, 0.4 mg ml−1. The investigation was carried out for two model surfaces: methylated silica (hydrophobic) and silica (hydrophilic and negatively charged, at pH 7). As a complement, a surface with a gradient in surface hydrophobicity was used. The end points of the gradient are similar to the methylated silica and silica surfaces with respect to hydrophobicity. All the surfactants adsorbed on the methylated silica surfaces, whereas only the cationic surfactants adsorbed on the silica surface. The adsorption of fibrinogen was 0.64 ± 0.03 μg cm−1 and 0.35 ± 0.03 μg cm−2 on the methylated silica and silica surfaces, respectively. Addition of surfactant led to a decrease in the amount of fibrinogen adsorbed on the methylated silica surface for all the surfactants, but only SDS affected the amounts adsorbed on the silica surfaces to any great extent. Despite the fact that the cationic surfactants adsorbed onto the silica surface, they did not affect the amount of fibrinogen adsorbed. The removal of protein decreased for the alkyltrimethylammonium bromides with increasing hydrophilicity of the gradient surfaces, and the amount of fibrinogen remaining after surfactant treatment decreased slightly for SDS. The effect of the chain length of the surfactant on elutability was small. The rate of removal of fibrinogen by the surfactants was found to be slower for SDS compared with the alkyltrimethylammonium bromides at the methylated silica surface, and at the hydrophobic end and in the intermediate part of the gradient.Adsorption from mixtures of surfactant and fibrinogen was also studied and the effects of cationic and anionic surfactants were quite different. The adsorption of fibrinogen was increased in the presence of the cationic surfactants, especially on the silica surface, but decreased in the presence of SDS. As surfactant adsorption onto clean surfaces is reversible with respect to dilution it might be assumed that the adsorbate mainly consists of fibrinogen. A trend was observed for the amounts of fibrinogen remaining after rinsing with buffer; the amounts increased with decreasing length of the surfactant hydrocarbon chain

Competition Between Fibrinogen and a Nonionic Surfactant at Adsorption to a Wettability Gradient Surface

The competition between mixtures of fibrinogen and a non-ionic surfactant (C12E5) with respect to adsorption onto a wettability gradient solid surface was studied by the use of ellipsometry. The effects of surface hydrophobicity and surfactant association were investigated. Furthermore the effect of clouding of the surfactant was studied by performing measurements at temperatures above and below the cloud point. At all concentrations, the fibrinogen (0.02–0.40 mg ml−1) was preferentially adsorbed onto the hydrophilic part of the gradient surface. At surfactant concentrations above and around the CMC, the protein was inhibited from adsorbing by the surfactant at the hydrophobic as well as in the intermediate part (50° ⩽ contact angle ⩽ 80°) of the gradient. As the surfactant concentrations was further reduced the protein was able to compete and adsorb onto the whole or parts of the gradient surface. In the case of a surfactant concentration of two-fifths of the CMC, the competitive power of the surfactant increased with temperature and the surfactant could hinder protein adsorption over a larger interval of the gradient surface. These observations were also verified by in situ measurements on non-gradient surfaces. The competition can be explained by considering the main interactions between protein and surfactant with the surface. In this respect cooperation in the self-association of the surfactant seems to be of great importance. The use of gradient surfaces makes it possible to observe subtle changes in these interactions

Protein/Emulsifier Interactions

An important consequence of protein-lipid interaction is the effect on stability of the protein in solution as well as on its behavior at interfaces. Here we will discuss key aspects of protein aggregation and unfolding as well as the effects of protein structure (random coil proteins versus globular) that are relevant for our understanding protein-lipid interaction. The main types of emulsifiers are the (1) aqueous soluble, surfactant type and (2) lipids with low aqueous solubility. The monomer concentration as defined by cmc is an important parameter for the soluble lipids. For emulsifiers with low aqueous solubility the emulsifier self-assembly structure and its properties control the interaction with proteins. We will therefore summarize the main features of lipid self-assembly. It also allows us to define different plausible scenarios and principles and models for factors that control the interactions in real food (and Pharmaceutical) systems. For the food applications the fate of the lipid during digestion is important and therefore we will discuss some aspects of enzyme-catalyzed lipolysis in terms of the structural evolution. New products and concepts of using protein/emulsifier interactions will be exemplified by illustrating how food nanotechnology possibly can be used for the delivery of functionality