Site-Specific Orientation of an α-Helical Peptide Ovispirin-1 from Isotope-Labeled SFG Spectroscopy

TitleSite-Specific Orientation of an α-Helical Peptide Ovispirin-1 from Isotope-Labeled SFG Spectroscopy
Publication TypeJournal Article
Year of Publication2013
AuthorsDing B, Laaser JE, Liu Y, Wang P, Zanni MT, Chen Z
Secondary TitleThe Journal of Physical Chemistry B
Volume117
Issue47
Pagination14625 - 14634
Date Published11/2013
Abstract

Sum-frequency generation (SFG) vibrational spectroscopy is often used to probe the backbone structures and orientations of polypeptides at surfaces. Using the ovispirin-1 polypeptide at the solid/liquid interface of polystyrene, we demonstrate for the first time that SFG can probe the polarization response of a single-isotope-labeled residue. To interpret the spectral intensities, we simulated the spectra using an excitonic Hamiltonian approach. We show that the polarization dependence of either the label or the unlabeled amide I band alone does not provide sufficient structural constraints to obtain both the tilt and the twist of the ovispirin helix at a solid/liquid interface, but that both can be determined from the polarization dependence of the complete spectrum. For ovispirin, the detailed analysis of the polarized SFG experimental data shows that the helix axis is tilted at roughly 138° from the surface normal, and the transition dipole of the isotope-labeled C═O group is tilted at 23° from the surface normal, with the hydrophobic region facing the polystyrene surface. We further demonstrate that the Hamiltonian approach is able to address the coupling effect and the structural disorder. For comparison, we also collected the FTIR spectrum of ovispirin under similar conditions, which reveals the enhanced sensitivity of SFG for structural studies of single monolayer peptide surfaces. Our study provides insight into how structural and environmental effects appear in SFG spectra of the amide I band and establishes that SFG of isotope-labeled peptides will be a powerful technique for elucidating secondary structures with residue-by-residue resolution.

URLhttp://pubs.acs.org/doi/abs/10.1021/jp408064b
DOI10.1021/jp408064b
Short TitleJ. Phys. Chem. B