Welcome to the new version of CaltechAUTHORS. Login is currently restricted to library staff. If you notice any issues, please email coda@library.caltech.edu
Published December 20, 2000 | public
Journal Article

Two-Dimensional Order in β-Sheet Peptide Monolayers

Abstract

Amphiphilic peptides comprising alternating hydrophilic and hydrophobic amino acid residues were designed to form super-secondary structures composed of self-assembled β-strands as monolayers at the air−water interface. Insights provided by in situ grazing-incidence X-ray diffraction (GIXD), surface pressure vs area isotherms, and Fourier transform infrared spectroscopy allow structural characterization of the assembled nanostructures and rational correlation with the peptide sequence. Peptides seven to seventeen amino acids in length were found to form crystalline arrays with coherence lengths in the range of 100 to 1000 Å. Two-dimensional registry of the self-assembled peptides was induced by placement of proline residues at the peptide termini. The films were found to intercalate ordered arrays of ions between juxtaposed β-sheet ribbons to generate peptide−ion composite phases.

Additional Information

Copyright © 2000 American Chemical Society. Received June 22, 2000. Publication Date (Web): November 30, 2000. We thank Dr. Suzanna Horvath for peptide synthesis, Dr. George Rossman for help in ATR infrared spectroscopy, and Dr. William Goddard and Dr. Tahir Cagin for providing the CERIUS2 applications. This work was supported by the United States−Israel Binational Science Foundation, the U.S. National Science Foundation, the Kimmelmann Center, the DanSync program of the Danish Natural Science Research Council, and the European Community under TMR-Contract ERBFMGECT950059. We thank HASYLAB for synchrotron beamtime.

Additional details

Created:
August 19, 2023
Modified:
October 19, 2023