Influence of transmembrane peptides on bilayers of phosphatidylcholines with different acyl chain lengths studied by solid-state NMR

Tomas Byström, Erik Strandberg, Frank A. Kovacs, Timothy A. Cross, Göran Lindblom

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

The molecular orientation in a lipid membrane of the peptide fragment VEYAGIALFFVAAVLTLWSMLQYLSAAR (phosphatidylglycerophosphate synthase (Pgs) peptide E) of an integral membrane protein, Pgs, in Escherichia coli has been investigated by solid-state 15N nuclear magnetic resonance (NMR) on macroscopically aligned lipid bilayers. The secondary structure of the peptide in lipid vesicles was determined by circular dichroism spectroscopy. Furthermore, the phase behaviour of the Pgs peptide E/dierucoylphosphatidylcholine (DEruPC)/water system was determined by 2H, 31P and 15N solid-state NMR spectroscopy. The phase behaviour obtained was then compared to that of the Pgs peptide E solubilised in dioleoylphosphatidylcholine and water that was previously studied by Morein et al. [Biophys. J. 73 (1997) 3078-3088]. This was aimed to answer the question whether a difference in the length of the hydrophobic part of this peptide and the hydrophobic thickness of the lipid bilayer (hydrophobic mismatch) will affect the phase behaviour. The peptide mostly has a transmembrane orientation and is in an α-helical conformation. An isotropic phase is formed in DEruPC with high peptide content (peptide/lipid molar ratio (p/l) ≥ 1:15) and high water content (≥ 50%, w/w) at 35°C. At 55 and 65°C an isotropic phase is induced at high water content (≥ 50%, w/w) at all peptide contents studied (no isotropic phase forms in the lipid/water system under the conditions in this study). At high peptide contents (p/l ≥ 1:15) an isotropic phase forms at 20 and 40% (w/w) of water at 55 and 65°C. A comparison of the phase behaviour of the two homologous lipid systems reveals striking similarities, although the thicknesses of the two lipid bilayers differ by 7 Å. This suggests that the rationalisation of the phase behaviour in terms of the hydrophobic mismatch is not applicable to these systems. The C-terminus of Pgs peptide E is amphiphilic and a considerable part of the peptide is situated outside the hydrophobic part of the bilayer, a property of the peptide that to a large extent will affect the lipid/peptide phase behaviour. (C) 2000 Elsevier Science B.V.

Original languageEnglish (US)
Pages (from-to)335-345
Number of pages11
JournalBiochimica et Biophysica Acta - Biomembranes
Volume1509
Issue number1-2
DOIs
StatePublished - Dec 20 2000

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Phosphatidylcholines
Chain length
CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase
Magnetic Resonance Spectroscopy
Nuclear magnetic resonance
Peptides
Phase behavior
Lipids
Lipid bilayers
Water
Lipid Bilayers
Water content
Circular dichroism spectroscopy
Peptide Fragments
Molecular orientation
Membrane Lipids
Circular Dichroism
Crystal orientation
Escherichia coli
Nuclear magnetic resonance spectroscopy

Keywords

  • Hydrophobic peptide
  • Lipid/peptide phase diagram
  • Membrane protein
  • N chemical shift
  • Nuclear magnetic resonance

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Cell Biology

Cite this

Influence of transmembrane peptides on bilayers of phosphatidylcholines with different acyl chain lengths studied by solid-state NMR. / Byström, Tomas; Strandberg, Erik; Kovacs, Frank A.; Cross, Timothy A.; Lindblom, Göran.

In: Biochimica et Biophysica Acta - Biomembranes, Vol. 1509, No. 1-2, 20.12.2000, p. 335-345.

Research output: Contribution to journalArticle

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AU - Cross, Timothy A.

AU - Lindblom, Göran

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N2 - The molecular orientation in a lipid membrane of the peptide fragment VEYAGIALFFVAAVLTLWSMLQYLSAAR (phosphatidylglycerophosphate synthase (Pgs) peptide E) of an integral membrane protein, Pgs, in Escherichia coli has been investigated by solid-state 15N nuclear magnetic resonance (NMR) on macroscopically aligned lipid bilayers. The secondary structure of the peptide in lipid vesicles was determined by circular dichroism spectroscopy. Furthermore, the phase behaviour of the Pgs peptide E/dierucoylphosphatidylcholine (DEruPC)/water system was determined by 2H, 31P and 15N solid-state NMR spectroscopy. The phase behaviour obtained was then compared to that of the Pgs peptide E solubilised in dioleoylphosphatidylcholine and water that was previously studied by Morein et al. [Biophys. J. 73 (1997) 3078-3088]. This was aimed to answer the question whether a difference in the length of the hydrophobic part of this peptide and the hydrophobic thickness of the lipid bilayer (hydrophobic mismatch) will affect the phase behaviour. The peptide mostly has a transmembrane orientation and is in an α-helical conformation. An isotropic phase is formed in DEruPC with high peptide content (peptide/lipid molar ratio (p/l) ≥ 1:15) and high water content (≥ 50%, w/w) at 35°C. At 55 and 65°C an isotropic phase is induced at high water content (≥ 50%, w/w) at all peptide contents studied (no isotropic phase forms in the lipid/water system under the conditions in this study). At high peptide contents (p/l ≥ 1:15) an isotropic phase forms at 20 and 40% (w/w) of water at 55 and 65°C. A comparison of the phase behaviour of the two homologous lipid systems reveals striking similarities, although the thicknesses of the two lipid bilayers differ by 7 Å. This suggests that the rationalisation of the phase behaviour in terms of the hydrophobic mismatch is not applicable to these systems. The C-terminus of Pgs peptide E is amphiphilic and a considerable part of the peptide is situated outside the hydrophobic part of the bilayer, a property of the peptide that to a large extent will affect the lipid/peptide phase behaviour. (C) 2000 Elsevier Science B.V.

AB - The molecular orientation in a lipid membrane of the peptide fragment VEYAGIALFFVAAVLTLWSMLQYLSAAR (phosphatidylglycerophosphate synthase (Pgs) peptide E) of an integral membrane protein, Pgs, in Escherichia coli has been investigated by solid-state 15N nuclear magnetic resonance (NMR) on macroscopically aligned lipid bilayers. The secondary structure of the peptide in lipid vesicles was determined by circular dichroism spectroscopy. Furthermore, the phase behaviour of the Pgs peptide E/dierucoylphosphatidylcholine (DEruPC)/water system was determined by 2H, 31P and 15N solid-state NMR spectroscopy. The phase behaviour obtained was then compared to that of the Pgs peptide E solubilised in dioleoylphosphatidylcholine and water that was previously studied by Morein et al. [Biophys. J. 73 (1997) 3078-3088]. This was aimed to answer the question whether a difference in the length of the hydrophobic part of this peptide and the hydrophobic thickness of the lipid bilayer (hydrophobic mismatch) will affect the phase behaviour. The peptide mostly has a transmembrane orientation and is in an α-helical conformation. An isotropic phase is formed in DEruPC with high peptide content (peptide/lipid molar ratio (p/l) ≥ 1:15) and high water content (≥ 50%, w/w) at 35°C. At 55 and 65°C an isotropic phase is induced at high water content (≥ 50%, w/w) at all peptide contents studied (no isotropic phase forms in the lipid/water system under the conditions in this study). At high peptide contents (p/l ≥ 1:15) an isotropic phase forms at 20 and 40% (w/w) of water at 55 and 65°C. A comparison of the phase behaviour of the two homologous lipid systems reveals striking similarities, although the thicknesses of the two lipid bilayers differ by 7 Å. This suggests that the rationalisation of the phase behaviour in terms of the hydrophobic mismatch is not applicable to these systems. The C-terminus of Pgs peptide E is amphiphilic and a considerable part of the peptide is situated outside the hydrophobic part of the bilayer, a property of the peptide that to a large extent will affect the lipid/peptide phase behaviour. (C) 2000 Elsevier Science B.V.

KW - Hydrophobic peptide

KW - Lipid/peptide phase diagram

KW - Membrane protein

KW - N chemical shift

KW - Nuclear magnetic resonance

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