Propensity for helix formation in the hydrophobic peptides K 2 (LA)(x) (x = 6, 8, 10, 12) in monolayer, bulk, and lipid-containing phases. Infrared and circular dichroism studies

Darline Dieudonné, Arne Gericke, Carol R. Flach, Xin Jiang, Ramy S. Farid, Richard Mendelsohn

Research output: Contribution to journalArticle

42 Citations (Scopus)

Abstract

A series of hydrophobic peptides K 2 (LA)(x) (x = 6, 8, 10, 12) has been synthesized. IR and CD studies in MeOH solution are reported, along with IR studies of these species in vesicles with 1,2-dipalmitoylphosphatidylcholine, and IR Reflection-Absorption-Spectroscopy (IRRAS) studies of peptide and lipid/peptide monolayer films in situ at the air/water interface. In bulk phases, the propensity toward helix formation increases with increasing chain length,there being essentially no helix in the shortest peptide, varying and concentration-dependent helical content in K 2 (LA) 8 , and >90% helix formation in both K 2 (LA) 10 and K 2 (LA) 12 . In monolayers at the air/water interface, peptide secondary structure was inferred from both the Amide I and Amide A bands. The shortest peptide adopted an antiparallel β-sheet structure, while the remainder of the series (when spread at low surface pressure) appeared to adopt varying proportions-of parallel-sheet forms. The secondary structure adopted by K 2 (LA) 10 and K 2 (LA) 12 depended remarkably on the initial spreading pressure; when spread at high pressures, the molecules were α-helical. The current experiments demonstrate the unique advantages of IRRAS for evaluation of peptide conformations in situ at the air/water interface and reveal large differences in the propensity for helix formation in monolayers compared with bulk phases.

Original languageEnglish (US)
Pages (from-to)792-799
Number of pages8
JournalJournal of the American Chemical Society
Volume120
Issue number4
DOIs
StatePublished - Feb 4 1998

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Dichroism
Circular Dichroism
Lipids
Peptides
Monolayers
Infrared radiation
Air
Absorption spectroscopy
Amides
Pressure
Water
Spectrum Analysis
1,2-Dipalmitoylphosphatidylcholine
Chain length
Conformations
Molecules

All Science Journal Classification (ASJC) codes

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

Cite this

@article{aee0520e42c14b4ea32c666a7e695e86,
title = "Propensity for helix formation in the hydrophobic peptides K 2 (LA)(x) (x = 6, 8, 10, 12) in monolayer, bulk, and lipid-containing phases. Infrared and circular dichroism studies",
abstract = "A series of hydrophobic peptides K 2 (LA)(x) (x = 6, 8, 10, 12) has been synthesized. IR and CD studies in MeOH solution are reported, along with IR studies of these species in vesicles with 1,2-dipalmitoylphosphatidylcholine, and IR Reflection-Absorption-Spectroscopy (IRRAS) studies of peptide and lipid/peptide monolayer films in situ at the air/water interface. In bulk phases, the propensity toward helix formation increases with increasing chain length,there being essentially no helix in the shortest peptide, varying and concentration-dependent helical content in K 2 (LA) 8 , and >90{\%} helix formation in both K 2 (LA) 10 and K 2 (LA) 12 . In monolayers at the air/water interface, peptide secondary structure was inferred from both the Amide I and Amide A bands. The shortest peptide adopted an antiparallel β-sheet structure, while the remainder of the series (when spread at low surface pressure) appeared to adopt varying proportions-of parallel-sheet forms. The secondary structure adopted by K 2 (LA) 10 and K 2 (LA) 12 depended remarkably on the initial spreading pressure; when spread at high pressures, the molecules were α-helical. The current experiments demonstrate the unique advantages of IRRAS for evaluation of peptide conformations in situ at the air/water interface and reveal large differences in the propensity for helix formation in monolayers compared with bulk phases.",
author = "Darline Dieudonn{\'e} and Arne Gericke and Flach, {Carol R.} and Xin Jiang and Farid, {Ramy S.} and Richard Mendelsohn",
year = "1998",
month = "2",
day = "4",
doi = "10.1021/ja9724046",
language = "English (US)",
volume = "120",
pages = "792--799",
journal = "Journal of the American Chemical Society",
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Propensity for helix formation in the hydrophobic peptides K 2 (LA)(x) (x = 6, 8, 10, 12) in monolayer, bulk, and lipid-containing phases. Infrared and circular dichroism studies . / Dieudonné, Darline; Gericke, Arne; Flach, Carol R.; Jiang, Xin; Farid, Ramy S.; Mendelsohn, Richard.

In: Journal of the American Chemical Society, Vol. 120, No. 4, 04.02.1998, p. 792-799.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Propensity for helix formation in the hydrophobic peptides K 2 (LA)(x) (x = 6, 8, 10, 12) in monolayer, bulk, and lipid-containing phases. Infrared and circular dichroism studies

AU - Dieudonné, Darline

AU - Gericke, Arne

AU - Flach, Carol R.

AU - Jiang, Xin

AU - Farid, Ramy S.

AU - Mendelsohn, Richard

PY - 1998/2/4

Y1 - 1998/2/4

N2 - A series of hydrophobic peptides K 2 (LA)(x) (x = 6, 8, 10, 12) has been synthesized. IR and CD studies in MeOH solution are reported, along with IR studies of these species in vesicles with 1,2-dipalmitoylphosphatidylcholine, and IR Reflection-Absorption-Spectroscopy (IRRAS) studies of peptide and lipid/peptide monolayer films in situ at the air/water interface. In bulk phases, the propensity toward helix formation increases with increasing chain length,there being essentially no helix in the shortest peptide, varying and concentration-dependent helical content in K 2 (LA) 8 , and >90% helix formation in both K 2 (LA) 10 and K 2 (LA) 12 . In monolayers at the air/water interface, peptide secondary structure was inferred from both the Amide I and Amide A bands. The shortest peptide adopted an antiparallel β-sheet structure, while the remainder of the series (when spread at low surface pressure) appeared to adopt varying proportions-of parallel-sheet forms. The secondary structure adopted by K 2 (LA) 10 and K 2 (LA) 12 depended remarkably on the initial spreading pressure; when spread at high pressures, the molecules were α-helical. The current experiments demonstrate the unique advantages of IRRAS for evaluation of peptide conformations in situ at the air/water interface and reveal large differences in the propensity for helix formation in monolayers compared with bulk phases.

AB - A series of hydrophobic peptides K 2 (LA)(x) (x = 6, 8, 10, 12) has been synthesized. IR and CD studies in MeOH solution are reported, along with IR studies of these species in vesicles with 1,2-dipalmitoylphosphatidylcholine, and IR Reflection-Absorption-Spectroscopy (IRRAS) studies of peptide and lipid/peptide monolayer films in situ at the air/water interface. In bulk phases, the propensity toward helix formation increases with increasing chain length,there being essentially no helix in the shortest peptide, varying and concentration-dependent helical content in K 2 (LA) 8 , and >90% helix formation in both K 2 (LA) 10 and K 2 (LA) 12 . In monolayers at the air/water interface, peptide secondary structure was inferred from both the Amide I and Amide A bands. The shortest peptide adopted an antiparallel β-sheet structure, while the remainder of the series (when spread at low surface pressure) appeared to adopt varying proportions-of parallel-sheet forms. The secondary structure adopted by K 2 (LA) 10 and K 2 (LA) 12 depended remarkably on the initial spreading pressure; when spread at high pressures, the molecules were α-helical. The current experiments demonstrate the unique advantages of IRRAS for evaluation of peptide conformations in situ at the air/water interface and reveal large differences in the propensity for helix formation in monolayers compared with bulk phases.

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SN - 0002-7863

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