Surface plasmon resonance analysis at a supported lipid monolayer

Matthew A. Cooper*, Andrew C. Try, Joe Carroll, David J. Ellar, Dudley H. Williams

*Corresponding author for this work

Research output: Contribution to journalArticle

116 Citations (Scopus)

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. Copyright (C) 1998 Elsevier Science B.V.

Original languageEnglish
Pages (from-to)101-111
Number of pages11
JournalBiochimica et Biophysica Acta - Biomembranes
Volume1373
Issue number1
DOIs
Publication statusPublished - 14 Aug 1998

Keywords

  • Aminopeptidase N
  • Cry1Ac
  • Glycopeptide antibiotic
  • Glycosylphosphatidylinositol
  • Kinetics
  • Lipid monolayer
  • Surface plasmon resonance
  • Toxin

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