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The interfacial structure and composition of water solutions with alkylimidazolium ionic liquids varying in their halide anions ([C12mim][X], X = Cl and I) were investigated by X-ray near-total-reflection fluorescence spectroscopy and X-ray reflectivity measurements. We demonstrate that X-ray fluorescence and reflectivity techniques provide a more direct measurement of surface adsorption. Furthermore, we show that for [C12mim][Cl] and [C12mim][I] solutions with mixed inorganic salts (NaI, NaCl), I(-) ions replace Cl(-) above the critical micelle concentration (CMC) of [C12mim][Cl] at much lower concentrations of NaI, whereas NaCl concentrations a hundred times higher than the CMC of [C12mim][I] only partially replace the I(-) at the interface. Our surface-sensitive X-ray diffraction and spectroscopy provide two independent tools to directly determine the surface adsorption of ionic surfactants and the interfacial composition of the surface films.

Three representative polymers of increasing modulus, poly(d,l-lactic acid), PDLLA, poly(desaminotyrosyl-tyrosine ethyl ester carbonate), PDTEC, and the same polymer with iodinated DTE segments, PI2DTEC, were characterized by surface-pressure versus area (Π-A) isotherms and surface sensitive X-ray diffraction techniques. Films of 10-100 Å thickness were prepared for these studies by spreading dilute polymer solutions at air-water interfaces. The general properties of the isotherms and the Flory exponents, determined from the isotherms, vary in accordance with the increasing modulus of PDLLA, PDTEC, PI2DTEC, respectively. The analysis of in situ X-ray reflectivity and grazing incidence X-ray diffraction (GIXD) measurements from films at aqueous surfaces provides a morphological picture that is consistent with the modulus of the polymers, and to a large extent, with their packing in their dry-bulk state. Large absorption of X-rays by iodine enabled X-ray spectroscopic studies under near-total-reflection conditions to determine the iodine distribution in the PI2DTEC film and complement the structural model derived from reflectivity and GIXD. These structural studies lay the foundation for future studies of polymer-protein interactions at aqueous interfaces.

In situ imaging ellipsometry is employed to monitor the morphology of collapsed films of fatty acid Langmuir monolayers on pure water and on CaCl2 solution. The ellipsometry images reveal the existence of multilayer domains in the collapsed region, and analysis of the images yields the thicknesses of these domains. The multilayer films formed on water are mainly trilayers, while those on CaCl2 solution are mainly bilayers. The structure of the collapsed films also changes sensitively depending on the history of compression of the molecular layer.

Near-resonance X-ray spectroscopy is used to determine ion distributions and their local environment at charged aqueous interfaces. Energy scans at fixed momentum-transfers under specular reflectivity conditions near the L(III) Cs(+) resonance reveal the formation of a diffuse Gouy-Chapman layer at a charged surface formed by a Langmuir monolayer (dihexadecyl phosphate) spread on CsI solution. The energy scans exhibit a periodic dependence on photon momentum-transfer (Q(z)) with a line-shape that consists of a Q(z)-dependent linear combination of the dispersive f'(E) and absorptive f''(E) fine-structure corrections. The results in the Born approximation are discussed and more quantitatively by using the dynamical method numerically (i.e. recursive or matrix methods to calculate the reflection of electromagnetic waves from stratified media). The ion distributions obtained from the analysis of the spectroscopy are in excellent agreement with those obtained from anomalous reflectivity measurements, providing further confirmation to the validity of the renormalized surface-charge Poisson-Boltzmann theory for monovalent ions. The fine structures of f'(E) and f''(E) obtained in the process differ significantly from the multi-electron photoexcitation spectra of the isolated ion, revealing the local environment of a Cs(+) ion in the solution at the interface. The comparison with similar X-ray absorption fine structures suggests that the Cs(+) ion is surrounded by a shell of eight O atoms.

Monomolecular films of valine gramicidin A (VGA) were investigated in situ at the air-water interface by x-ray reflectivity and x-ray grazing incidence diffraction as well as polarization modulation infrared reflection absorption spectroscopy (PM-IRRAS). These techniques were combined to obtain information on the secondary structure and the orientation of VGA and to characterize the shoulder observed in its pi-A isotherm. The thickness of the film was obtained by x-ray reflectivity, and the secondary structure of VGA was monitored using the frequency position of the amide I band. The PM-IRRAS spectra were compared with the simulated ones to identify the conformation adopted by VGA in monolayer. At large molecular area, VGA shows a disordered secondary structure, whereas at smaller molecular areas, VGA adopts an anti-parallel double-strand intertwined beta(5.6) helical conformation with 30 degrees orientation with respect to the normal with a thickness of 25 A. The interface between bulk water and the VGA monolayer was investigated by x-ray reflectivity as well as by comparing the experimental and the simulated PM-IRRAS spectra on D(2)O and H(2)O, which suggested the presence of oriented water molecules between the bulk and the monolayer.

Monomolecular films of the membrane protein rhodopsin have been investigated in situ at the air-water interface by polarization modulation infrared reflection absorption spectroscopy (PM-IRRAS) and X-ray reflectivity in order to find conditions that retain the protein secondary structure. The spreading of rhodopsin at 0 or 5 mN m(-1) followed by a 30 min incubation time at 21 degrees C resulted in the unfolding of rhodopsin, as evidenced from the large increase of its molecular area, its small monolayer thickness, and the extensive formation of beta-sheets at the expense of the alpha-helices originally present in rhodopsin. In contrast, when spreading is performed at 5 or 10 mN m(-1) followed by an immediate compression at, respectively, 4 or 21 degrees C, the secondary structure of rhodopsin is retained, and the thickness of these films is in good agreement with the size of rhodopsin determined from its crystal structure. The amide I/amide II ratio also allowed to determine that the orientation of rhodopsin only slightly changes with surface pressure and it remains almost unchanged when the film is maintained at 20 mN m(-1) for 120 min at 4 degrees C. In addition, the PM-IRRAS spectra of rod outer segment disk membranes in monolayers suggest that rhodopsin also retained its secondary structure in these films.

X-ray fluorescence spectra from monovalent ions (Cs+) that accumulate from dilute solutions to form an ion-rich layer near a charged Langmuir monolayer are presented. For the salt solution without the monolayer, the fluorescence signals below the critical angle are significantly lower than the detection sensitivity and only above the critical angle signals from the bulk are observed. In the presence of a monolayer that provides surface charges, strong fluorescence signals below the critical angle are observed. Ion density accumulated at the interface are determined from the fluorescence. The fluorescent spectra collected as a function of incident x-ray energy near the LIII edge yield the extended absorption spectra from the ions, and are compared to recent independent results. The fluorescence data from divalent Ba2+ with and without monolayer are also presented. [ABSTRACT FROM AUTHOR]

We show that the structure factor S(q) of water can be obtained from x-ray synchrotron experiments at grazing angle of incidence (in reflection mode) by using a liquid surface diffractometer. The corrections used to obtain S(q) self-consistently are described. Applying these corrections to scans at different incident beam angles (above the critical angle) collapses the measured intensities into a single master curve, without fitting parameters, which within a scale factor yields S(q). Performing the measurements below the critical angle for total reflectivity yields the structure factor of the top most layers of the water/vapor interface. Our results indicate water restructuring at the vapor/water interface. We also introduce a new approach to extract g(r), the pair distribution function (PDF), by expressing the PDF as a linear sum of error functions whose parameters are refined by applying a nonlinear least square fit method. This approach enables a straightforward determination of the inherent uncertainties in the PDF. Implications of our results to previously measured and theoretical predictions of the PDF are also discussed. [ABSTRACT FROM AUTHOR]

X-ray reflectivity (XR) and grazing incident-angle x-ray diffraction (GIXD) reveal that sphingomyelin, although forming homogeneous monomolecular films at air–water interfaces, does not develop long-range crystalline in-plane order at any in-plane density, most notably at high surface pressures where many other membrane lipids order as two-dimensional crystals. Studies were carried out on the monodisperse synthetic C18-sphingomyelin where both hydrocarbon chains are saturated and on natural sphingomyelin which contains a distribution of chain lengths, with saturated and unsaturated hydrocarbon chains. The surface pressure versus molecular area (π–A) isotherm for the natural sphingomyelin is similar to that of the synthetic, but has a somewhat higher surface pressure at intermediate areas. The absence of in-plane crystalline order is attributed to competing interactions in the head group region: hydrogen bonding in the erythro region, electrostatic interactions among zwitterions of neighboring head groups, and van der Waals among acyl chains. © 2001 American Institute of Physics. [ABSTRACT FROM AUTHOR]