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Sorting of lipids and transmembrane peptides between detergent-soluble bilayers and detergent-resistant rafts.

Publication ,  Journal Article
McIntosh, TJ; Vidal, A; Simon, SA
Published in: Biophys J
September 2003

Specific proteins and lipids sequester to regions of cell membranes called rafts. Due to their high content of sphingomyelin (SM) and cholesterol, raft bilayers are thicker than nonraft bilayers and, at least at 4 degrees C, are resistant to Triton X-100 extraction. It has been postulated that rafts concentrate proteins with long transbilayer domains because of "hydrophobic matching" between the transbilayer domain and the thick bilayer hydrocarbon region. However, because the area compressibility and bending moduli of SM:cholesterol bilayers are larger than that of nonraft bilayers, there should be an energy cost to partition proteins or peptides into rafts. To determine the effects on peptide sorting of raft thickness and mechanical properties, we incorporated two transbilayer peptides (P-23, P-29) into bilayers composed of SM, dioleoylphosphatidylcholine, and cholesterol, separated detergent-soluble membranes (DSMs) from detergent-resistant membranes (DRMs), and measured their peptide and lipid compositions. P-23 and P-29 were designed to have transbilayer domains that matched the hydrocarbon thicknesses of DSMs and DRMs, respectively. At both 4 degrees C and 37 degrees C DSMs were enriched in dioleoylphosphatidylcholine and DRMs were enriched in SM and cholesterol. At both temperatures both P-23 and P-29 preferentially localized to DSMs, demonstrating the importance of bilayer mechanical properties relative to hydrophobic mismatch. However, at 37 degrees C significantly more P-29 than P-23 was located in DRMs, implying that hydrophobic matching played a role in peptide sorting at physiological temperature. These experiments demonstrate that the sorting of peptides as measured by detergent extraction is temperature-dependent and both bilayer mechanical properties and hydrophobic matching impact peptide distribution between DSMs and DRMs.

Duke Scholars

Published In

Biophys J

DOI

ISSN

0006-3495

Publication Date

September 2003

Volume

85

Issue

3

Start / End Page

1656 / 1666

Location

United States

Related Subject Headings

  • Thermodynamics
  • Temperature
  • Sphingomyelins
  • Phosphatidylcholines
  • Peptides
  • Octoxynol
  • Models, Biological
  • Membrane Microdomains
  • Lipids
  • Lipid Bilayers
 

Citation

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McIntosh, T. J., Vidal, A., & Simon, S. A. (2003). Sorting of lipids and transmembrane peptides between detergent-soluble bilayers and detergent-resistant rafts. Biophys J, 85(3), 1656–1666. https://doi.org/10.1016/S0006-3495(03)74595-0
McIntosh, Thomas J., Adriana Vidal, and Sidney A. Simon. “Sorting of lipids and transmembrane peptides between detergent-soluble bilayers and detergent-resistant rafts.Biophys J 85, no. 3 (September 2003): 1656–66. https://doi.org/10.1016/S0006-3495(03)74595-0.
McIntosh, Thomas J., et al. “Sorting of lipids and transmembrane peptides between detergent-soluble bilayers and detergent-resistant rafts.Biophys J, vol. 85, no. 3, Sept. 2003, pp. 1656–66. Pubmed, doi:10.1016/S0006-3495(03)74595-0.
Journal cover image

Published In

Biophys J

DOI

ISSN

0006-3495

Publication Date

September 2003

Volume

85

Issue

3

Start / End Page

1656 / 1666

Location

United States

Related Subject Headings

  • Thermodynamics
  • Temperature
  • Sphingomyelins
  • Phosphatidylcholines
  • Peptides
  • Octoxynol
  • Models, Biological
  • Membrane Microdomains
  • Lipids
  • Lipid Bilayers