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    Crystalline Cyclic Peptide Nanotubes at Interfaces

    Year: 1999

    Journal: J. Am. Chem. Soc. 1999, 121, 1186-1191, 20111221

    Authors: Hanna Rapaport, Hui Sun Kim, Kristian Kjaer, Paul B. Howes, Sidney Cohen, Jens Als-Nielsen, M. Reza Ghadiri, Leslie Leiserowitz, and Meir Lahav

    Organizations: Contribution from the Department of Materials and Interfaces, Weizmann Institute of Science, Rehovot 76100, Israel, Department of Solid State Physics, Risi National Laboratory, DK-4000 Roskilde, Denmark, Niels Bohr Institute, H. C. Øersted Laboratory, Universitetsparken 5, DK-2100 Copenhagen, Denmark, and Department of Chemistry & Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California 92037

    The assembly, orientation, and structural features of nanoscale tubes composed of cyclic peptides, formed at the air-water interface, were detected by grazing incidence X-ray diffraction (GIXD). The peptide cyclo-[(L-Phe-D-N-MeAla-)4] (1) exhibits two-dimensional crystallinity in which the plane of the peptide ring is parallel to the water interface. The peptide cyclo-[(L-Trp-D-Leu)3-L-Ser-D-Leu] (2) forms predominantly planar aggregates composed of several tubes, lying with their long axes parallel to the air-water interface. In contrast, the peptide cyclo-[(L-Trp-D-Leu)4] (3) exhibits a very low tendency to form ordered two-dimensional arrays of nanotubes. Films of peptides 2 and 3 as well as their mixtures with the phospholipid DPPA were transferred onto a solid support and visualized by scanning force microscopy (SFM).