Cationic surfactants, protein

Quaternary ammonium compounds are cationic surfactants that bind well to anionic surfaces like the protein in hair. The ammonium end sticks to the hair, leaving the long fatty end of the molecule to act as a lubricant. They are slightly conductive, so they reduce the buildup of static electricity. Quats, as they are sometimes called, include compounds like stearalkonium chloride, disteardimonium chloride, quaternium-5, or quaternium-18, polyquaternium-10 and they are all similar in form and function to cetrimonium chloride. These compounds are also widely used as fabric softeners, for all of the same reasons they make good hair conditioners. They are also used to thicken the shampoo. 

Ejfect of pH It is obvious that in order to recover the protein from reverse micelles, the pH of the stripping solution needs to change toward the pi, which will result in a reduction of the protein interaction with the oppositely charged head groups. The extent of protein recovery from reverse micelles increases with increasing pH for anionic surfactants however, for cationic surfactants the opposite is true. 

Disinfectants come from various chemical classes, including oxidants, halogens or halogen-releasing agents, alcohols, aldehydes, organic acids, phenols, cationic surfactants (detergents) and formerly also heavy metals. The basic mechanisms of action involve de-naturation of proteins, inhibition of enzymes, or a dehydration. Effects are dependent on concentration and contact time. 

Small ACTH fragments related to ACTH-(4-10) have also been investigated for the presence of ordered structure. CD of ACTH--(5-10) in TFE showed a random structure (50) as was found with H-NMR for fragment 4-10 (51). The addition of anionic or cationic surfactants to an aqueous solution of ACTH-(4-11) dit not promote any a-helix or 3-form in this peptide (CD experiments S2). When ACTH-(1-14) and 1-10 were measured by CD and NMR respectively, indications for a helical or ordered structure were found (90, ). Thus it seems that the addition of the non-helix "prone" fragment 1-3 or 1-4 can promote the formation of a helical structure in the adjacent sequence. Arguments in favour of this come from the theoretical work of Argos and Palau (53) on amino acid distribution in protein secondary structures. They found that Ser and Thr frequently occur at the N-terminal helical position (cf. Ser in ACTH) to provide stability the position adjacent to the helical C-terminus is often occupied by Gly or Pro (adjacent toTrp in ACTH we have Gly ) acidic amino acid residues are frequently found at the helix N-terminus (cf. Glu in ACTH) and/or basic residues at the C-terminus (cf. Arg ). 

When the wall is made hydrophobic by treatment with alkylsilane, it is possible to separate proteins that tend to adsorb at the surface of bare fused silica. Ultimately, it is possible to recuperate one type of ion depending on the direction of the electric field. Finally, if a cationic surfactant is added to reverse the polarity of the inner wall, it is possible to reverse the direction of the electro-osmotic flow (Fig. 8.6). 

Various authors have shown that non-ionic surfactants have a beneficial effect on the hydrolysis of cellulosic and lignocellulosic substrates, whereas anionic and cationic surfactants alone interfere negatively (Castanon and Wilke, 1981 Helle et al, 1993 Park et al, 1992 Ooshima et al., 1986 Traore and Buschle-Diller, 1999 Ueda el al., 1994 Eriksson el al., 2002). Increases in the amount of reducing soluble sugars and substrate conversion were reported. The effect depends on the substrate and is not observed for soluble substrates, such as carboxymethylcellulose or cellobiose. Nonionic surfactants increased the initial rate of hydrolysis of Sigmacell 100, and when they were added later in the process they were less effective (Helle et al, 1993). They same authors found also that the addition of cellulose increases the critical micelle concentration of the surfactant, which indicates that the surfactant adsorbs to the substrate. Surfactants are more effective at lower enzyme loads and reduce the amount of adsorbed protein (Castanon and Wilke, 1981 Ooshima et al, 1986 Helle et al, 1993 Eriksson et al., 2002) which can be used to increase desorption of cellulase from the cellulosic substrate (Otter et al., 1989). Anyhow, the use of surfactants to enhance desorption of cellulases from textile substrates in order to recover and recycle cellulases was not successful (Azevedo et al., 2002b). 

Most systems examined to date have employed the AOT anionic reversed micellar system (366-370). In one case, amylase was extracted using trioctylmethylammonium chloride (cationic surfactant) in isooctane (375) while in another, catalase was extracted using a cationic DTAB/octane/hexanol reversed micelle (377). In our own research, we have successfully employed nonionic Igepal CO-530 -CCl, cationic CTAB - hexanol, and zwitterionic lecithin - CC1, reversed micellar systems in the extraction of some amino acids and proteins (379). The availability of such a pool of different charge-type micellar systems allows one flexibility in the development of such extraction schemes. In fact, preliminary results seem to indicate that better extractions are obtainable in some instances via use of zwitterionic reversed micellar media (379). 

Proteins solubilized in aqueous solution interact more or less with hydrophilic groups of surfactants at the oil-water interface. Therefore, the type of hydrophilic group is strongly influenced by the protein extraction efficiency. Anionic and cationic surfactants interact with charged protein surfaces more strongly than non-ionic surfactants. This feature also means that the non-ionic surfactants are favourable for protein stabilization in water droplets because of the not-so-hard interaction between the protein and the surfactant. In protein extraction, such an electrostatic interaction between proteins and surfactants is the main driving force in protein transfer. 

In the protein extraction by reverse micelles, it is well known that the selection of surfactants is very important and often determines the success of the protein extraction operation [9]. In the initial stage of our experiments, we chose the cationic surfactant TOMAC. It is easy to deduce that cationic surfactants are the best candidates for DNA extraction because DNA is negatively charged and behaves as a polyanion in an intermediate pH solution. Meanwhile TOMAC is a typical and effective cationic surfactant for protein extraction by reverse micelles [23]. However, the reverse micelles that are formed by TOMAC cannot extract DNA in the organic solvent, although the concentration of DNA in the aqueous phase is reduced. A similar tendency is observed when CTAB is employed. The effect of the surfactants on the DNA extraction is summarized in Table 14.3. 

The functionalization of the reverse micelles will create a novel application in bioseparation processes in the analytical and medical sciences. It is therefore important to reveal the recognition mechanism of proteins at the liquid-liquid interface in reversed micellar solutions. DNA is also successfully extracted in a few hours by reversed micelles formed by cationic surfactants in isooctane. The driving force of the DNA transfer is the electrostatic interaction between the cationic surfactants and the negatively charged DNA. Another important factor is the hydrophobicity of the cationic surfactants. Doublechain type cationic surfactants are found to be one of the best surfactants ensuring the efficient extraction of DNA. These results have shown that reverse micellar solutions will become a useful tool not only for protein separation, but also for DNA separation. 

Most cubic phases in lipid-water systems exhibit unit cell parameters not larger than 20 mn, while the imit cell of cubic membranes is usually larger than 100 nm. Some exceptioi have been apparently found [131, 132] although at this stage such findings should be treated with caution, as the determination of lattice parameters is dependent on the indexing of diffraction patterns, based only on a small niunber of reflections. Further, in lipid-protein-water, lipid-poloxamer-water and lipid-cationic surfactant-water systems, cubic phases with cell parameters of the order of 50 nm have been observed [56,127, 128]. Due to the small number of reports dealing with the... 

Cationic surfactants and protonated polyamines may reverse the direction of the EOF as they impart a positive charge on the capillary wall. This technique is used to prevent wall interactions with cationic proteins. Changing the direction of the EOF is important in anion analysis where comigration of anions and the EOF is required. Otherwise, highly mobile anions such as chloride migrate toward the anode, whereas lower mobility anions are swept by the EOF toward the cathode. 

Influent concentrations and residual concentrations of cationic surfactants, anionic surfactants, cationic polyelectrolyte, anionic polyelectrolyte, proteins, colloids, oxygen, ozone, detergents, suspended sohds, and so on, in the adsorptive bubble separation systems can be determined by the analytical methods reported in the literature (82,127-149). 

Persson A, Chang D, Crouch E. Surfactant protein D is a divalent cation-dependent carbohydrate-binding protein. J Biol Chem 1990 265 5755-60. 

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