Hydrophobic interactions preferential interaction

Separations in hydrophobic interaction chromatography have been modeled as a function of the ionic strength of the buffer and of the hydrophobicity of the column, and tested using the elution of lysozyme and ovalbumin from octyl-, butyl- and phenyl-Sepharose phases.2 The theoretical framework used preferential interaction analysis, a theory competitive to solvophobic theory. Solvophobic theory views protein-surface interaction as a two-step process. In this model, the protein appears in a cavity in the water formed above the adsorption site and then adsorbs to the phase, with the free energy change... 

One of the component mechanisms is, of course, hydrophobic interactions. Retention is proportional to column hydrophobicity, and elution order is expected to generally follow solute hydrophobicity. However, it is important to keep in mind that proteins bind preferentially to columns by their dominantly hydrophobic surface. Two proteins with very similar average surface hydrophobicity may exhibit very different retention characteristics due to differences in their respective distribution of hydrophobic residues.1,2... 

The theoretical treatment of the hydrophobic effect is limited to pure aqueous systems. To describe chromatographic separations in RPC Horvath and Melander developed the solvophobic theory [47]. In this theory, no special assumptions are made about the properties of solute and solvent, and besides hydrophobic interaction electrostatic and other specific interactions are included. The theory has been valuable to describe the retention of nonpolar [48], polar [49], and ionizable [50] solutes in RPC. The modulation of selectivity via secondary equilibria (variation of pH, ion pair formation [51]) can also be described. On the other hand, it is not a problem to find examples of dispersive interactions in literature, e.g., separation of carotinoids with a long chain (C30) RP gives a higher selectivity compared to standard RP C18 cyclohexanols are preferentially retarded on cyclohexyl-bonded phases compared to phases with linear-bonded alkyl groups. 

A more sophisticated class of optical sensors with high selectivity towards ions are the ion-selective optodes (ISOs) [21], where the matrix (hydrophobic polymer such as PVC) contains a selective lipophilic ionophore (optically silent), a chromoionophore, a plasticizer and an anionic additive. The measurement principle is based on a thermodynamic equilibrium that controls the ion exchange (for sensing cations) or ion coextraction (for sensing anions) with the sample. The source of optode selectivity is a preferential interaction between the target ion and an ionophore. For a dye to act as a chromoionophore, it must... 

As earlier reported for electrochemical sensing, often the active chromo-phore will be dispersed in a polymeric matrix. For example, Mohr and Wolfbeis reported a nitrate sensor [121] where the active chromophore is a rhodamine B dye which had been modified with an octadecyl side chain to render it hydrophobic and prevent leaching. The dye was dispersed in a plasticised PVC membrane containing a hydrophobic anion carrier (tridodecylmethylammo-nium chloride). On exposure to nitrate, the fluorescence of the dye increased. This membrane, however, only displayed Hofmeister-type selectivity and was also affected by pH. Replacing the quaternary ammonium anion carrier with a palladium phospine chloride carrier led to selectivity for nitrite [ 122], probably due to a preferential interaction between Pd and nitrite ion. 

The addition of polyhydroxyl compounds to enzyme solutions have been shown to increase the stabilities of enzymes, (13,16,19,20). This is thought to be due to the interaction of the polyhydroxyl compound, (e.g. sucrose, polyethylene glycols, sugar alcohols, etc), with water in the system. This effectively reduces the protein - water interactions as the polyhydroxy compounds become preferentially hydrated and thus die hydrophobic interactions of the protein structure are effectively strengthened. This leads to an increased resistance to thermal denaturadon of the protein structure, and in the case of enzymes, an increase in the stability of the enzyme, shown by retention of enzymic activity at temperatures at which unmodified aqueous enzyme solutions are deactivated. 

Several classes of potent and selective inhibitors of NEP and APN have been rationally designed. The specificity of NEP is essentially ensured by the Si subsite, which interacts preferentially with aromatic or large hydrophobic moieties, whereas the S2 subsite has a poor specificity [13]. These observations were used to design thiorphan [14] and retrothiorphan [15], which were the first described potent synthetic NEP inhibitors. Protection of the thiol and carboxyl groups of thiorphan led to acetorphan, a compound able to cross the blood-brain barrier (BBB) after systemic administration. Various natural APN inhibitors have been isolated, some of them exhibiting relatively good... 

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