Laser spectroscopy of conformational constrained α/β-peptides: Ac-ACPC-Phe-NHMe and Ac-Phe-ACPC-NHMe

William H. James, Esteban E. Baquero, Soo Hyuk Choi, Samuel H. Gellman, Timothy S. Zwier

Research output: Contribution to journalArticle

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Abstract

Single-conformation ultraviolet and infrared spectra have been recorded under the isolated molecule conditions of a supersonic expansion for three conformationally constrained α/β-peptides, Ac-L-Phe-ACPC-NHMe (αLβACPC). Ac-ACPC-L-Phe-NHMe (βACPCαL), and Ac-ACPC-D-Phe-NHMe (βACPCαD)- These three molecules are close analogues of the hAla-containing α/β-peptide counterparts Ac-L-Phe-β3-hAla-NHMe, Ac-3-hAla-L-Phe-NHMe, and Ac-/β3-hAla-D-Phe-NHMe, which have been studied recently by James et al. (J. Am. Chem. Soc. 2009, 131.,6574). Incorporation of β-amino acid trans-2-aminocyclopentanecarboxylic acid (ACPC) constrains the β-peptide backbone via the cyclopentane ring, producing clear changes in the conformational preferences relative to the unconstrained analogues. The conformational control is manifested most obviously in the complete absence of C6 H-bonded rings, which were dominant in the unconstrained α/β- peptides. The most stable C6 ring structure (C6a) in the absence of the ACPC ring cannot be formed in its presence, while a secondary C6 ring (C6b) has its energy destabilized by ∼20 kJ/mol. In αLβ ACPC the preference for C5 structures in the N-terminal position, combined with the strong preference for C8 structures in the β-peptide subunit, leads to the observation of two C5/C8 bifurcated double ring conformers. Both C8/C7 sequential double rings and C11 single rings are observed in βACPCαL and βACPCα D Here, the ACPC ring selectively stabilizes the C8a ring over other possible C8 structures. Finally, the combined evidence from IR and UV spectra lead to tentative assignments for diastereomeric pairs, exhibiting small but understandable shifts in the IR and UV spectra nduced by the change in chirality at the α-peptide chiral center.

Original languageEnglish
Pages (from-to)1581-1591
Number of pages11
JournalJournal of Physical Chemistry A
Volume114
Issue number3
DOIs
Publication statusPublished - 2010 Mar 1

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Cycloleucine
Laser spectroscopy
laser spectroscopy
peptides
Peptides
acids
rings
Cyclopentanes
analogs
Molecules
Chirality
ring structures
ultraviolet spectra
Conformations
chirality
amino acids
molecules
infrared spectra
Infrared radiation
Amino Acids

All Science Journal Classification (ASJC) codes

  • Physical and Theoretical Chemistry

Cite this

James, William H. ; Baquero, Esteban E. ; Choi, Soo Hyuk ; Gellman, Samuel H. ; Zwier, Timothy S. / Laser spectroscopy of conformational constrained α/β-peptides : Ac-ACPC-Phe-NHMe and Ac-Phe-ACPC-NHMe. In: Journal of Physical Chemistry A. 2010 ; Vol. 114, No. 3. pp. 1581-1591.
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title = "Laser spectroscopy of conformational constrained α/β-peptides: Ac-ACPC-Phe-NHMe and Ac-Phe-ACPC-NHMe",
abstract = "Single-conformation ultraviolet and infrared spectra have been recorded under the isolated molecule conditions of a supersonic expansion for three conformationally constrained α/β-peptides, Ac-L-Phe-ACPC-NHMe (αLβACPC). Ac-ACPC-L-Phe-NHMe (βACPCαL), and Ac-ACPC-D-Phe-NHMe (βACPCαD)- These three molecules are close analogues of the hAla-containing α/β-peptide counterparts Ac-L-Phe-β3-hAla-NHMe, Ac-3-hAla-L-Phe-NHMe, and Ac-/β3-hAla-D-Phe-NHMe, which have been studied recently by James et al. (J. Am. Chem. Soc. 2009, 131.,6574). Incorporation of β-amino acid trans-2-aminocyclopentanecarboxylic acid (ACPC) constrains the β-peptide backbone via the cyclopentane ring, producing clear changes in the conformational preferences relative to the unconstrained analogues. The conformational control is manifested most obviously in the complete absence of C6 H-bonded rings, which were dominant in the unconstrained α/β- peptides. The most stable C6 ring structure (C6a) in the absence of the ACPC ring cannot be formed in its presence, while a secondary C6 ring (C6b) has its energy destabilized by ∼20 kJ/mol. In αLβ ACPC the preference for C5 structures in the N-terminal position, combined with the strong preference for C8 structures in the β-peptide subunit, leads to the observation of two C5/C8 bifurcated double ring conformers. Both C8/C7 sequential double rings and C11 single rings are observed in βACPCαL and βACPCα D Here, the ACPC ring selectively stabilizes the C8a ring over other possible C8 structures. Finally, the combined evidence from IR and UV spectra lead to tentative assignments for diastereomeric pairs, exhibiting small but understandable shifts in the IR and UV spectra nduced by the change in chirality at the α-peptide chiral center.",
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Laser spectroscopy of conformational constrained α/β-peptides : Ac-ACPC-Phe-NHMe and Ac-Phe-ACPC-NHMe. / James, William H.; Baquero, Esteban E.; Choi, Soo Hyuk; Gellman, Samuel H.; Zwier, Timothy S.

In: Journal of Physical Chemistry A, Vol. 114, No. 3, 01.03.2010, p. 1581-1591.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Laser spectroscopy of conformational constrained α/β-peptides

T2 - Ac-ACPC-Phe-NHMe and Ac-Phe-ACPC-NHMe

AU - James, William H.

AU - Baquero, Esteban E.

AU - Choi, Soo Hyuk

AU - Gellman, Samuel H.

AU - Zwier, Timothy S.

PY - 2010/3/1

Y1 - 2010/3/1

N2 - Single-conformation ultraviolet and infrared spectra have been recorded under the isolated molecule conditions of a supersonic expansion for three conformationally constrained α/β-peptides, Ac-L-Phe-ACPC-NHMe (αLβACPC). Ac-ACPC-L-Phe-NHMe (βACPCαL), and Ac-ACPC-D-Phe-NHMe (βACPCαD)- These three molecules are close analogues of the hAla-containing α/β-peptide counterparts Ac-L-Phe-β3-hAla-NHMe, Ac-3-hAla-L-Phe-NHMe, and Ac-/β3-hAla-D-Phe-NHMe, which have been studied recently by James et al. (J. Am. Chem. Soc. 2009, 131.,6574). Incorporation of β-amino acid trans-2-aminocyclopentanecarboxylic acid (ACPC) constrains the β-peptide backbone via the cyclopentane ring, producing clear changes in the conformational preferences relative to the unconstrained analogues. The conformational control is manifested most obviously in the complete absence of C6 H-bonded rings, which were dominant in the unconstrained α/β- peptides. The most stable C6 ring structure (C6a) in the absence of the ACPC ring cannot be formed in its presence, while a secondary C6 ring (C6b) has its energy destabilized by ∼20 kJ/mol. In αLβ ACPC the preference for C5 structures in the N-terminal position, combined with the strong preference for C8 structures in the β-peptide subunit, leads to the observation of two C5/C8 bifurcated double ring conformers. Both C8/C7 sequential double rings and C11 single rings are observed in βACPCαL and βACPCα D Here, the ACPC ring selectively stabilizes the C8a ring over other possible C8 structures. Finally, the combined evidence from IR and UV spectra lead to tentative assignments for diastereomeric pairs, exhibiting small but understandable shifts in the IR and UV spectra nduced by the change in chirality at the α-peptide chiral center.

AB - Single-conformation ultraviolet and infrared spectra have been recorded under the isolated molecule conditions of a supersonic expansion for three conformationally constrained α/β-peptides, Ac-L-Phe-ACPC-NHMe (αLβACPC). Ac-ACPC-L-Phe-NHMe (βACPCαL), and Ac-ACPC-D-Phe-NHMe (βACPCαD)- These three molecules are close analogues of the hAla-containing α/β-peptide counterparts Ac-L-Phe-β3-hAla-NHMe, Ac-3-hAla-L-Phe-NHMe, and Ac-/β3-hAla-D-Phe-NHMe, which have been studied recently by James et al. (J. Am. Chem. Soc. 2009, 131.,6574). Incorporation of β-amino acid trans-2-aminocyclopentanecarboxylic acid (ACPC) constrains the β-peptide backbone via the cyclopentane ring, producing clear changes in the conformational preferences relative to the unconstrained analogues. The conformational control is manifested most obviously in the complete absence of C6 H-bonded rings, which were dominant in the unconstrained α/β- peptides. The most stable C6 ring structure (C6a) in the absence of the ACPC ring cannot be formed in its presence, while a secondary C6 ring (C6b) has its energy destabilized by ∼20 kJ/mol. In αLβ ACPC the preference for C5 structures in the N-terminal position, combined with the strong preference for C8 structures in the β-peptide subunit, leads to the observation of two C5/C8 bifurcated double ring conformers. Both C8/C7 sequential double rings and C11 single rings are observed in βACPCαL and βACPCα D Here, the ACPC ring selectively stabilizes the C8a ring over other possible C8 structures. Finally, the combined evidence from IR and UV spectra lead to tentative assignments for diastereomeric pairs, exhibiting small but understandable shifts in the IR and UV spectra nduced by the change in chirality at the α-peptide chiral center.

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