Intramolecular interactions in protonated peptides: H+PheGlyGly and H+GlyGlyPhe

Timothy D. Vaden; Tjalling S.J.A. De Boer; John P. Simons; Lavina C. Snoek

doi:10.1039/b716666d

Intramolecular interactions in protonated peptides: H⁺PheGlyGly and H⁺GlyGlyPhe

Timothy D. Vaden, Tjalling S.J.A. De Boer, John P. Simons, Lavina C. Snoek

Research output: Contribution to journal › Article › peer-review

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Abstract

The conformations of protonated PheGlyGly and GlyGlyPhe tripeptides, generated at temperatures ∼300-350 K through a photochemical mechanism, were investigated in the gas phase using R-IRMPD spectroscopy in the OH and NH stretch region in combination with quantum chemistry calculations. The results aid characterisation of their conformational landscapes and specifically, help identify the intramolecular interactions that control the peptide conformations. The dominant intramolecular interaction in protonated PheGlyGly operates between the N-and C-termini but in protonated GlyGlyPhe there is a strong cation-π interaction. The observation of a cation-π interaction in the warm ions highlights its strong, stable nature.

Original language	English (US)
Pages (from-to)	1443-1447
Number of pages	5
Journal	Physical Chemistry Chemical Physics
Volume	10
Issue number	10
DOIs	https://doi.org/10.1039/b716666d
State	Published - Mar 7 2008

All Science Journal Classification (ASJC) codes

Physics and Astronomy(all)
Physical and Theoretical Chemistry

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abstract = "The conformations of protonated PheGlyGly and GlyGlyPhe tripeptides, generated at temperatures ∼300-350 K through a photochemical mechanism, were investigated in the gas phase using R-IRMPD spectroscopy in the OH and NH stretch region in combination with quantum chemistry calculations. The results aid characterisation of their conformational landscapes and specifically, help identify the intramolecular interactions that control the peptide conformations. The dominant intramolecular interaction in protonated PheGlyGly operates between the N-and C-termini but in protonated GlyGlyPhe there is a strong cation-π interaction. The observation of a cation-π interaction in the warm ions highlights its strong, stable nature.",

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AU - Vaden, Timothy D.

AU - De Boer, Tjalling S.J.A.

AU - Simons, John P.

AU - Snoek, Lavina C.

PY - 2008/3/7

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AB - The conformations of protonated PheGlyGly and GlyGlyPhe tripeptides, generated at temperatures ∼300-350 K through a photochemical mechanism, were investigated in the gas phase using R-IRMPD spectroscopy in the OH and NH stretch region in combination with quantum chemistry calculations. The results aid characterisation of their conformational landscapes and specifically, help identify the intramolecular interactions that control the peptide conformations. The dominant intramolecular interaction in protonated PheGlyGly operates between the N-and C-termini but in protonated GlyGlyPhe there is a strong cation-π interaction. The observation of a cation-π interaction in the warm ions highlights its strong, stable nature.

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Intramolecular interactions in protonated peptides: H⁺PheGlyGly and H⁺GlyGlyPhe

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