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Assembly and structure of α-helical peptide films on hydrophobic fluorocarbon surfaces
Biointerphases volume 5, pages 9–16 (2010)
Abstract
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.
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Weidner, T., Samuel, N.T., McCrea, K. et al. Assembly and structure of α-helical peptide films on hydrophobic fluorocarbon surfaces. Biointerphases 5, 9–16 (2010). https://doi.org/10.1116/1.3317116
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DOI: https://doi.org/10.1116/1.3317116