Micellar packing

Fig. 22.1 Phase diagram for the micellar packing of the surfactant cetyltrimethylammonium bromide changing with respect to temperature and surfactant concentration. (Reprinted with permission from ACS journals )...

The experimental-theoretical study of mesophase formation in amphiphilic systems emphasizes the basic chemical, physical, and materials science aspects of the systems. The most commonly discussed mesophases, beyond the simple micelles discussed in Chapter 4, are lamellar aggregated micellar (packed in various cubic and hexagonal close-packed arrays), columnar or ribbon phases (rod-shaped micelles stacked in a two-dimensional hexagonal or rectangular array) microemulsions, and the cubic bicontinuous mesophases. The experimental techniques normally used to identify these mesophases are NMR Uneshape analysis, diffusion measurements, smaU-angle neutron and X-ray scattering, and optical texture analyses. In addition, reconstraction of electron density profiles and very low temperature transmission electron microscopy (TEM) have been used to elucidate the details of these mesostractures. 

Micellization is a second-order or continuous type phase transition. Therefore, one observes continuous changes over the course of micelle fonnation. Many experimental teclmiques are particularly well suited for examining properties of micelles and micellar solutions. Important micellar properties include micelle size and aggregation number, self-diffusion coefficient, molecular packing of surfactant in the micelle, extent of surfactant ionization and counterion binding affinity, micelle collision rates, and many others. 

The early Hartley model [2, 3] of a spherical micellar stmcture resulted, in later years, in some considerable debate. The self-consistency (inconsistency) of spherical symmetry witli molecular packing constraints was subsequently noted [4, 5 and 6]. There is now no serious question of tlie tenet tliat unswollen micelles may readily deviate from spherical geometry, and ellipsoidal geometries are now commonly reported. Many micelles are essentially spherical, however, as deduced from many light and neutron scattering studies. Even ellipsoidal objects will appear... 

In otlier words, tire micelle surface is not densely packed witli headgroups, but also comprises intennediate and end of chain segments of tire tailgroups. Such segments reasonably interact witli water, consistent witli dynamical measurements. Given tliat tire lifetime of individual surfactants in micelles is of tire order of microseconds and tliat of micelles is of tire order of milliseconds, it is clear tliat tire dynamical equilibria associated witli micellar stmctures is one tliat brings most segments of surfactant into contact witli water. The core of nonnal micelles probably remains fairly dry , however. 

Kovat s retention index (p. 575) liquid-solid adsorption chromatography (p. 590) longitudinal diffusion (p. 560) loop injector (p. 584) mass spectrum (p. 571) mass transfer (p. 561) micellar electrokinetic capillary chromatography (p. 606) micelle (p. 606) mobile phase (p. 546) normal-phase chromatography (p. 580) on-column injection (p. 568) open tubular column (p. 564) packed column (p. 564) peak capacity (p. 554)... 

FIG. 1 Self-assembled structures in amphiphilic systems micellar structures (a) and (b) exist in aqueous solution as well as in ternary oil/water/amphiphile mixtures. In the latter case, they are swollen by the oil on the hydrophobic (tail) side. Monolayers (c) separate water from oil domains in ternary systems. Lipids in water tend to form bilayers (d) rather than micelles, since their hydrophobic block (two chains) is so compact and bulky, compared to the head group, that they cannot easily pack into a sphere [4]. At small concentrations, bilayers often close up to form vesicles (e). Some surfactants also form cyhndrical (wormlike) micelles (not shown). 

The conformation of bovine myelin basic protein (MBP) in AOT/isooctane/water reversed micellar systems was studied by Waks et al. 67). This MBP is an extrinsic water soluble protein which attains an extended conformation in aqueous solution 68 but is more density packed at the membrane surface. The solubilization of MBP in the AOT reversed micelles depends on the water/AOT-ratio w0 68). The maximum of solubilization was observed at a w0-value as low as 5.56. The same value was obtained for another major protein component of myelin, the Folch-Pi proteolipid 69). According to fluorescence emission spectra of MBP, accessibility of the single tryptophane residue seems to be decreased in AOT reversed micelles. From CD-spectra one can conclude that there is a higher conformational rigidity in reversed micelles and a more ordered aqueous environment. 

By and NMR, the occurrence of conformational changes of the AOT molecules with R has been emphasized [13]. An increase of the lateral packing order of the surfactant alkyl chains located in the micellar palisade layer due to water addition has also been pointed out by FT-IR [58,92]. 

Scheme 1 gives a representation of an approximately spherical micelle in water, with ionic head groups at the surface and counterions clustered around the micelle partially neutralizing the charges. Counterions which are closely associated with the micelle can be assumed to be located in a shell, the so-called Stern layer, the thickness of which should be similar to the size of the micellar head groups. Monomeric co-ions will be repelled by the ionic head groups. The hydrophobic alkyl groups pack randomly and parts of the chains are exposed to water at the surface (Section 2). 

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