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• W2026348767 endingPage "3440" @default.
• W2026348767 startingPage "3433" @default.
• W2026348767 abstract "The structure and orientation of amphiphilic α-helix and β-strand model peptide films on self-assembled monolayers (SAMs) have been studied with sum frequency generation (SFG) vibrational spectroscopy and near-edge X-ray absorption fine structure (NEXAFS) spectroscopy. The α-helix peptide is a 14-mer, and the β-strand is a 15-mer of hydrophilic lysine and hydrophobic leucine residues with hydrophobic periodicities of 3.5 and 2, respectively. These periodicities result in the leucine side chains located on one side of the peptides and the lysine side chains on the other side. The SAMs were prepared from the assembly of either carboxylic acid- or methyl-terminated alkyl thiols onto gold surfaces. For SFG studies, the deuterated analog of the methyl SAM was used. SFG vibrational spectra in the C−H region of air-dried peptides films on both SAMs exhibit strong peaks near 2965, 2940, and 2875 cm−1 related to ordered leucine side chains. The orientation of the leucine side chains was determined from the phase of these features relative to the nonresonant gold background. The relative phase for both the α-helix and β-strand peptides showed that the leucine side chains were oriented away from the carboxylic acid SAM surface and oriented toward the methyl SAM surface. Amide I peaks observed near 1656 cm−1 for the α-helix peptide confirm that the secondary structure is preserved on both SAMs. Strong linear dichroism related to the amide π* orbital at 400.8 eV was observed in the nitrogen K-edge NEXAFS spectra for the adsorbed β-strand peptides, suggesting that the peptide backbones are oriented parallel to the SAM surface with the side chains pointing toward or away from the interface. For the α-helix the dichroism of the amide π* is significantly weaker, probably because of the broad distribution of amide bond orientations in the α-helix secondary structure." @default.
• W2026348767 created "2016-06-24" @default.
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• W2026348767 date "2009-11-05" @default.
• W2026348767 modified "2023-10-07" @default.
• W2026348767 title "Probing the Orientation and Conformation of α-Helix and β-Strand Model Peptides on Self-Assembled Monolayers Using Sum Frequency Generation and NEXAFS Spectroscopy" @default.
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• W2026348767 doi "https://doi.org/10.1021/la903267x" @default.
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