Journal for Biophysical Chemistry

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Open Access

Assembly and structure of α-helical peptide films on hydrophobic fluorocarbon surfaces

  • Tobias Weidner1,
  • Newton T. Samuel1, 2,
  • Keith McCrea3,
  • Lara J. Gamble1,
  • Robert S. Ward3 and
  • David G. Castner1Email author

Received: 31 December 2009

Accepted: 16 January 2010


The structure, orientation, and formation of amphiphilic α-helix model peptide films on fluorocarbon surfaces has been monitored with sum frequency generation (SFG) vibrational spectroscopy, near-edge x-ray absorption fine structure (NEXAFS) spectroscopy, and x-ray photoelectron spectroscopy (XPS). The α-helix peptide is a 14-mer of hydrophilic lysine and hydrophobic leucine residues with a hydrophobic periodicity of 3.5. This periodicity yields a rigid amphiphilic peptide with leucine and lysine side chains located on opposite sides. XPS composition analysis confirms the formation of a peptide film that covers about 75% of the surface. NEXAFS data are consistent with chemically intact adsorption of the peptides. A weak linear dichroism of the amide π is likely due to the broad distribution of amide bond orientations inherent to the α-helical secondary structure. SFG spectra exhibit strong peaks near 2865 and 2935 cm−1 related to aligned leucine side chains interacting with the hydrophobic surface. Water modes near 3200 and 3400 cm−1 indicate ordering of water molecules in the adsorbed-peptide fluorocarbon surface interfacial region. Amide I peaks observed near 1655 cm−1 confirm that the secondary structure is preserved in the adsorbed peptide. A kinetic study of the film formation process using XPS and SFG showed rapid adsorption of the peptides followed by a longer assembly process. Peptide SFG spectra taken at the air-buffer interface showed features related to well-ordered peptide films. Moving samples through the buffer surface led to the transfer of ordered peptide films onto the substrates.