Betaines (a particular class of amphoteric surfactants) are commonly used as foam boosters in various products to improve their foamability and foam stability. Foaming media often contain dispersed drops of silicone or hydrocarbon oil, which act as foam destruction agents (antifoams). A complementary set of experiments on foams and foam films stabilized by an anionic surfactant, sodium dodecyl-polyoxyethylene-3-sulfate (SDP3S), or by mixtures of SDP3S and Betaine, is performed in the present study to clarify the mechanisms of:  (1) foam destruction by silicone oil drops, and (2) foam boosting effect of betaine in the presence of oil. The experiments show that foams stabilized by SDP3S are very stable in the absence of oil, while they are unstable and decay with time in the presence of oil (antifoam effect of the oil). The introduction of 40 molar % betaine in the mixture leads to complete foam stabilization in both caseswith and without oil (foam boosting effect). Notably, the size of the oil droplets has a significant effect on the foam stabilitya substantial amount of silicone oil can be introduced without deteriorating the foam stability, if the drop diameter is below ca. 5 μm. Optical observations of the process of foam film thinning show that the oil drops leave the films without destroying them in all of the studied systems (stable and unstable) relatively soon after foam formationtypically, within less than a minute. The foam destruction occurs at a later stage of the foam evolution, when the oil drops are compressed by the walls of the narrowing Plateau channels as a result of liquid drainage from the foam. Surface and interfacial tension measurements show that variations in the values of entry, E, spreading, S, and bridging, B, coefficients cannot be used to explain the observed foam boosting effect of betaine. On the other hand, direct measurements of the critical capillary pressure leading to drop entry demonstrate that the barrier to drop entry is much higher in the presence of betaine. The data unambiguously show that the main role of betaine as a foam booster in the studied systems is to increase the barrier to drop entry, which leads to suppressed activity of the silicone oil as an antifoam. The obtained results provide deeper insight into the foam boosting effect and suggest some clues about the properties which an efficient booster should possess.

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In this study, we compared domain formation in raftlike mixtures of cholesterol and dioleoylphosphatidylcholine (DOPC) with either sphingomyelin (SM) or dipalmitoylphosphatidylcholine (DPPC). Using 2 H nuclear magnetic resonance, we studied the properties of the lipid enriched in the £uid phase, DOPC. We found that acyl chain 2 H-labeled DOPC is much less ordered in SM-containing mixtures than in those containing DPPC, suggesting that DOPC in the SM-containing mixture senses a lower concentration of cholesterol in its direct environment. Atomic force microscopy experiments demonstrated large di¡erences in the size and shape of domains in the di¡erent mixtures. We propose that these various di¡erences are a consequence of the preferential interaction of cholesterol for sphingolipids over glycerophospholipids.

Transmembrane (TM) alpha-helical peptides with neutral flanking residues such as tryptophan form highly ordered striated domains when incorporated in gel-state 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) bilayers and inspected by atomic force microscopy (AFM) (1). In this study, we analyze the molecular organization of these striated domains using AFM, photo-cross-linking, fluorescence spectroscopy, nuclear magnetic resonance (NMR), and X-ray diffraction techniques on different functionalized TM peptides. The results demonstrate that the striated domains consist of linear arrays of single TM peptides with a dominantly antiparallel organization in which the peptides interact with each other and with lipids. The peptide arrays are regularly spaced by +/-8.5 nm and are separated by somewhat perturbed gel-state lipids with hexagonally organized acyl chains, which have lost their tilt. This system provides an example of how domains of peptides and lipids can be formed in membranes as a result of a combination of specific peptide-peptide and peptide-lipid interactions.

In this study, we investigated the size and orientation of the bacterial Lipid II (L II) headgroup when the L II molecule is present in liquid-crystalline domains of DOPC in a supported DPPC bilayer. Using atomic force microscopy, we detected that L II causes the appearance of a 1.9 nm thick layer, situated over the DOPC headgroup region. With an increased scanning force, this layer can be penetrated by the AFM tip down to the level of the DOPC bilayer. Using different L II precursor molecules, we demonstrated that the detected layer consists of the headgroups of L II and that the MurNAc-pentapeptide unit of the headgroup is responsible for the measured 1.9 nm height of that layer. Monolayer experiments provided information about the in-plane dimensions of the L II headgroup. On the basis of these results and considerations of the molecular dimensions of L II headgroup constituents, we propose a model for the orientation of the L II headgroup in the membrane. In this model, the pentapeptide of the L II headgroup is rather extended and points away from the bilayer surface, which could be important for biological processes, in which L II is involved.