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Cross-Strand Coupling of a β-Hairpin Peptide Stabilized with an Aib-Gly Turn Studied Using Isotope-Edited IR Spectroscopy

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Contribution from the Department of Chemistry, University of Illinois at Chicago, 845 West Taylor Street (m/c111), Chicago, Illinois 60607-7061, Department of Chemistry, Louisiana State University, 232 Choppin Hall, Baton Rouge, Louisiana 70803-1804
Cite this: J. Am. Chem. Soc. 2007, 129, 44, 13592–13603
Publication Date (Web):October 11, 2007
https://doi.org/10.1021/ja0736414
Copyright © 2007 American Chemical Society

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    Abstract

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    Isotope-edited IR spectroscopy was used to study a series of singly and doubly 13CO-labeled β-hairpin peptides stabilized by an Aib-Gly turn sequence. The double-labeled peptides have amide I‘ IR spectra that show different degrees of vibrational coupling between the 13C-labeled amides due to variations in the local geometry of the peptide structure. The single-labeled peptides provide controls to determine frequencies characteristic of the diagonal force field (FF) contributions at each position for the uncoupled 13CO modes. Separation of diagonal FF and coupling effects on the spectra are used to explain the cross-strand labeled spectral patterns. DFT calculations based on an idealized model β-hairpin peptide correctly predict the vibrational coupling patterns. Extending these model results by consideration of frayed ends and the hairpin conformational flexibility yields an alternate interpretation of details of the spectra. Temperature-dependent isotopically labeled IR spectra reveal differences in the thermal stabilities of the individual isotopically labeled sites. This is the first example of using an IR-based isotopic labeling technique to differentiate structural transitions at specific sites along the peptide backbone in model β-hairpin peptides.

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     University of Illinois at Chicago.

    §

     Current address:  Department of Analytical Chemistry, Institute of Chemical Technology, Technicka 5, 166 28 Prague 6, Czech Republic.

     Louisiana State University.

     Current address:  Department of Chemistry, University of Wyoming, Laramie, WY, 82071.

    *

    In papers with more than one author, the asterisk indicates the name of the author to whom inquiries about the paper should be addressed.

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    Detailed results from MD simulations, QM spectral calulations, and temperature-dependent IR spectra for the unlabeled and single-labeled peptides. This material is available free of charge via the Internet at http://pubs.acs.org.

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