Characterizing peptide β-hairpin loops via cold ion spectroscopy of model compounds

Lawler, John T.

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https://hdl.handle.net/2142/96939 Copy

Description

Title

Characterizing peptide β-hairpin loops via cold ion spectroscopy of model compounds

Author(s)

Lawler, John T.

Contributor(s)

• Zwier, Timothy S.
• McLuckey, Scott A.
• Fischer, Joshua L.
• Harrilal, Christopher P.
• DeBlase, Andrew F.

Issue Date

2017-06-23

Keyword(s)

Ions

Abstract

The introduction of non-native D-amino acids into peptides is known to reduce conformational entropy in peptides. D-proline has been shown to promote the formation of $beta$-hairpin loops when paired with Gly, providing a framework for building these loops with different lengths of anti-parallel beta-sheet. This study seeks to characterize and compare the conformational preferences of a model protonated pentapeptide containing DPG, [YAP$^{D}$GA+H]$^{+}$, with its L-Pro counterpart via conformation specific cold ion spectroscopy as a foundation for future consideration of larger beta-hairpin models._x000d_ _x000d_ The UV spectrum of YAP$^{D}$GA of the Tyr chromophore is beautifully sharp, but contains a complicated set of transitions that could arise from the presence of more than one conformer. To assess this possibility, we recorded non-conformation specific IR “gain” spectra in the hydride stretch region. The IR spectrum so obtained displays a set of five strong IR transitions that bear a close resemblance to those found in one of the conformers of its close analog, [YAP$^{D}$AA+H]$^{+}$, signaling that a single conformer dominates the population. Two transitions at 3392 and 3464 cm-1 are slightly shifted versions of the C10 and C14 hydrogen bonds found in one of the conformers of [YAP$^{D}$AA+H]$^{+}$, and are characteristic of formation of a $beta$-hairpin loop. Notably, in [YAP$^{D}$GA+H]$^{+}$, there is at most a minor second conformer with a free carboxylic acid OH, appearing weakly in the IR “gain” spectrum. As expected, the UV spectrum of YAP$^{L}$GA is more congested, which suggests the presence of multiple conformers. Further investigation into this peptide will reveal the conformational preferences of the L-pro containing molecule. Preliminary data affirms that D-proline containing peptides show reduced conformational states when compared to their natural counterparts. _x000d_

Publisher

International Symposium on Molecular Spectroscopy

Type of Resource

text

Language

eng

Permalink

http://hdl.handle.net/2142/96939

DOI

https://doi.org/10.15278/isms.2017.FE06

Copyright and License Information

Copyright 2017 John T. Lawler

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