Do interstrand hydrogen bonds contribute to β-hairpin peptide stability in solution? IR analysis of peptide folding in water

Christopher S. Colley; Samuel R. Griffiths-Jones; Michael W. George; Mark S. Searle

doi:10.1039/b000426j

Do interstrand hydrogen bonds contribute to β-hairpin peptide stability in solution? IR analysis of peptide folding in water

Christopher S. Colley, Samuel R. Griffiths-Jones, Michael W. George, Mark S. Searle

Research output: Journal Publication › Article › peer-review

24 Citations (Scopus)

Abstract

The amide I carbonyl stretch in the IR spectrum, together with ¹H NMR Hα chemical shifts, have been used to investigate the folding of a 16- residue β-hairpin peptide in water: while Hα shifts are consistent with a significant population of the folded state (ca. 40%), we see no features in the IR spectrum in the amide I region to suggest a significant contribution from interstrand hydrogen bonds, although at high peptide concentration (≥10 mM) the appearance of a new band at 1616 cm^-1 is consistent with the onset of irreversible peptide aggregation.

Original language	English
Pages (from-to)	593-594
Number of pages	2
Journal	Chemical Communications
Issue number	7
DOIs	https://doi.org/10.1039/b000426j
Publication status	Published - 7 Apr 2000
Externally published	Yes

ASJC Scopus subject areas

Catalysis
Electronic, Optical and Magnetic Materials
Ceramics and Composites
General Chemistry
Surfaces, Coatings and Films
Metals and Alloys
Materials Chemistry

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10.1039/b000426j

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abstract = "The amide I carbonyl stretch in the IR spectrum, together with 1H NMR Hα chemical shifts, have been used to investigate the folding of a 16- residue β-hairpin peptide in water: while Hα shifts are consistent with a significant population of the folded state (ca. 40\%), we see no features in the IR spectrum in the amide I region to suggest a significant contribution from interstrand hydrogen bonds, although at high peptide concentration (≥10 mM) the appearance of a new band at 1616 cm-1 is consistent with the onset of irreversible peptide aggregation.",

author = "Colley, \{Christopher S.\} and Griffiths-Jones, \{Samuel R.\} and George, \{Michael W.\} and Searle, \{Mark S.\}",

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AU - Colley, Christopher S.

AU - Griffiths-Jones, Samuel R.

AU - George, Michael W.

AU - Searle, Mark S.

PY - 2000/4/7

Y1 - 2000/4/7

N2 - The amide I carbonyl stretch in the IR spectrum, together with 1H NMR Hα chemical shifts, have been used to investigate the folding of a 16- residue β-hairpin peptide in water: while Hα shifts are consistent with a significant population of the folded state (ca. 40%), we see no features in the IR spectrum in the amide I region to suggest a significant contribution from interstrand hydrogen bonds, although at high peptide concentration (≥10 mM) the appearance of a new band at 1616 cm-1 is consistent with the onset of irreversible peptide aggregation.

AB - The amide I carbonyl stretch in the IR spectrum, together with 1H NMR Hα chemical shifts, have been used to investigate the folding of a 16- residue β-hairpin peptide in water: while Hα shifts are consistent with a significant population of the folded state (ca. 40%), we see no features in the IR spectrum in the amide I region to suggest a significant contribution from interstrand hydrogen bonds, although at high peptide concentration (≥10 mM) the appearance of a new band at 1616 cm-1 is consistent with the onset of irreversible peptide aggregation.

UR - https://www.scopus.com/pages/publications/0034616105

U2 - 10.1039/b000426j

DO - 10.1039/b000426j

M3 - Article

AN - SCOPUS:0034616105

SN - 1359-7345

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EP - 594

JO - Chemical Communications

JF - Chemical Communications

IS - 7

ER -

Do interstrand hydrogen bonds contribute to β-hairpin peptide stability in solution? IR analysis of peptide folding in water

Abstract

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