Hydrophilic surface hydrophobicity

Surfactant—solid and surfactant—surfactant hydrophobic interactions lead to minimization of solid—water and surfactant-chain—water contact and are energetically favorable. Unlike hydrophilic surfaces, hydrophobic surfaces do not lead to significant structuring of interfacial water, and the interfacial water is displaced from the surface relatively easily by the surfactant molecules. Consequently, surfactant adsorption on hydrophobic surfaces has often been found to be higher than adsorption on the corresponding hydrophilic surfaces (39, 54, 56, 57, 59—62), provided aqueous phase salinity is low. 

Diamond behaves somewhat differently in that n is low in air, about 0.1. It is dependent, however, on which crystal face is involved, and rises severalfold in vacuum (after heating) [1,2,25]. The behavior of sapphire is similar [24]. Diamond surfaces, incidentally, can have an oxide layer. Naturally occurring ones may be hydrophilic or hydrophobic, depending on whether they are found in formations exposed to air and water. The relation between surface wettability and friction seems not to have been studied. 

The nature of soliite-solnte and solute-solvent in teraction s is dependent on the solvent environment. Solvent influences the hydrogen-bon ding pattern, solute surface area, and hydrophilic and hydrophobic group exposures. 

Hydrophilic and Hydrophobic Surfaces. Water is a small, highly polar molecular and it is therefore strongly adsorbed on a polar surface as a result of the large contribution from the electrostatic forces. Polar adsorbents such as most zeoHtes, siUca gel, or activated alumina therefore adsorb water more strongly than they adsorb organic species, and, as a result, such adsorbents are commonly called hydrophilic. In contrast, on a nonpolar surface where there is no electrostatic interaction water is held only very weakly and is easily displaced by organics. Such adsorbents, which are the only practical choice for adsorption of organics from aqueous solutions, are termed hydrophobic. 

Lecithin (qv), a natural phosphoHpid possessing both hydrophilic and hydrophobic properties, is the most common emulsifier in the chocolate industry (5). The hydrophilic groups of the lecithin molecules attach themselves to the water, sugar, and cocoa soflds present in chocolate. The hydrophobic groups attach themselves to the cocoa butter and other fats such as milk fat. This reduces both the surface tension, between cocoa butter and the other materials present, and the viscosity. Less cocoa butter is then needed to adjust the final viscosity of the chocolate. 

Most molded plastics have a very smooth, hydrophobic surface that must be modified. Chemical etchants are used to oxidize and roughen the surface. The resultant hydrophilic surface promotes good metal-to-plastic adhesion. The etchant is usually a solution of chromic acid and sulfuric acid pure chromic acid can also be used. 

Lesk and Chothia did find, however, that there is a striking preferential conservation of the hydrophobic character of the amino acids at the 59 buried positions, but that no such conservation occurs at positions exposed on the surface of the molecule. With a few exceptions on the surface, hydrophobic residues have replaced hydrophilic ones and vice versa. However, the case of sickle-cell hemoglobin, which is described below, shows that a charge balance must be preserved to avoid hydrophobic patches on the surface. In summary, the evolutionary divergence of these nine globins has been constrained primarily by an almost absolute conservation of the hydro-phobicity of the residues buried in the helix-to-helix and helix-to-heme contacts. 

Figure 12.2 (a) Schematic drawing of membrane proteins in a typical membrane and their solubilization by detergents. The hydrophilic surfaces of the membrane proteins are indicated by red. (b) A membrane protein crystallized with detergents bound to its hydrophobic protein surface. The hydrophilic surfaces of the proteins and the symbols for detergents are as in (a). (Adapted from H. Michel, Trends Biochem. Sci. 8 56-59, 1983.)... 

Proteins derive their powerful and diverse capacity for molecular recognition and catalysis from their ability to fold into defined secondary and tertiary structures and display specific functional groups at precise locations in space. Functional protein domains are typically 50-200 residues in length and utilize a specific sequence of side chains to encode folded structures that have a compact hydrophobic core and a hydrophilic surface. Mimicry of protein structure and function by non-natural ohgomers such as peptoids wiU not only require the synthesis of >50mers with a variety of side chains, but wiU also require these non-natural sequences to adopt, in water, tertiary structures that are rich in secondary structure. 

The term "bioenertness" is a relative one since few if any synthetic polymers are totally biocompatible with living tissues. The terra is used here on the basis of preUminary in vitro and in vivo tests, together with chemical evaluations based on analogies with other well-tested systems. Two different types of polyphosphazenes are of interest as bioinert materials those with strongly hydrophobic surface characteristics and those with hydrophilic surfaces. These will be considered in turn. 

The connection between hydrophobicity and tissue compatibility has been noted for classical organic polymers (19). A key feature of the polyphosphazene substitutive synthesis method is the ease with which the surface hydrophobicity or hydrophilicity can be fine-tuned by variations in the ratios of two or more different side groups. It can also be varied by chemical reactions carried out on the organo-phosphazene polymer molecules themselves or on the surfaces of the solid materials. 

Intuitively it might be supposed that a poljrmer with a hydrophilic surface might be more biocompatible than one with a ("foreign ) hydrophobic surface. This simple interpretation is not always correct. Nevertheless, the study of hydrophilic polymers, especially those that promote endothelial tissue overgrowth or ingrowth, is an area of great interest. 

Water is a special liquid that forms unique bonds involving protons between the oxygen atoms of neighboring molecules, the so-called hydrogen bond. The solvation forces are then due not simply to molecular size effects, but also and most importantly to the directional nature of the bond. They can be attractive or hydrophobic (hydration forces between two hydrophobic surfaces) and repulsive or hydrophilic (between two hydrophilic surfaces). These forces arise from the disruption or modification of the hydrogen-bonding network of water by the surfaces. These forces are also found to decay exponentially with distance [6]. 

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