Surface plasmon resonance analysis at a supported lipid monolayer

Biochim Biophys Acta. 1998 Aug 14;1373(1):101-11. doi: 10.1016/s0005-2736(98)00091-1.

Abstract

Methods for the formation of supported lipid monolayers on top of a hydrophobic self assembled monolayer in a surface plasmon resonance instrument are described. Small unilamellar vesicles absorb spontaneously to the surface of the hydrophobic self-assembled monolayer to form a surface which resembles the surface of a cellular membrane. Lipophilic ligands, such as small acylated peptides or glycosylphosphatidylinositol-anchored proteins, were inserted into the absorbed lipid and binding of analytes to these ligands was analysed by surface plasmon resonance. Conditions for the formation of lipid monolayers have been optimised with respect to lipid type, chemical and buffer compatibility, ligand stability and reproducibility.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Anti-Bacterial Agents / metabolism
  • Bacillus thuringiensis Toxins
  • Bacterial Proteins / metabolism
  • Bacterial Toxins*
  • Endotoxins / metabolism
  • Glycopeptides
  • Glycosylphosphatidylinositols / chemistry
  • Glycosylphosphatidylinositols / metabolism
  • Hemolysin Proteins
  • Lipid Metabolism
  • Lipids / chemistry*
  • Magnetic Resonance Spectroscopy
  • Protein Binding
  • Reproducibility of Results
  • Spectrum Analysis / methods*

Substances

  • Anti-Bacterial Agents
  • Bacillus thuringiensis Toxins
  • Bacterial Proteins
  • Bacterial Toxins
  • Endotoxins
  • Glycopeptides
  • Glycosylphosphatidylinositols
  • Hemolysin Proteins
  • Lipids
  • insecticidal crystal protein, Bacillus Thuringiensis