Abstract
Recently it has been demonstrated that a compressed monolayer of palmitoyl-(R)-lysine (Fig. 1) on the surface of water induces the orientated growth of α-glyeine crystals1. This effect was inter-preted to be a structural match between the monolayer and the α-glycine. To test this hypothesis we undertook to determine the packing arrangement of the monolayer by grazing incidence X-ray diffraction and reflection. These techniques2 use the unique proper-ties of synchrotron radiation: high intensity within a small natural collimation3. In the diffraction experiment two peaks were detect-able in the two-dimensional powder pattern from a monolayer of palmitoyl-(R)-lysine. The positions and intensities of these peaks allowed us to choose between various models and determine the monolayer structure. This is the first time that the crystal structure of a compressed surfactant monolayer at the air–water interface has been determined. The same techniques could be used for structural characterization of other monolayers of interest in fields as diverse as biological membranes4 and optical second harmonic generation5. The packing arrangement of the α-amino acid head groups in the model proved to be very similar to that found in the crystal structures of α-glycine and several hydrophobic α-amino acids.
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Wolf, S., Leiserowitz, L., Lahav, M. et al. Elucidation of the two-dimensional structure of an α-amino acid surfactant monolayer on water using synchrotron X-ray diffraction. Nature 328, 63–66 (1987). https://doi.org/10.1038/328063a0
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DOI: https://doi.org/10.1038/328063a0
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