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 language | English |
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Pages (from-to) | 101-111 |
Number of pages | 11 |
Journal | Biochimica et Biophysica Acta - Biomembranes |
Volume | 1373 |
Issue number | 1 |
DOIs | |
Publication status | Published - 14 Aug 1998 |
Keywords
- Aminopeptidase N
- Cry1Ac
- Glycopeptide antibiotic
- Glycosylphosphatidylinositol
- Kinetics
- Lipid monolayer
- Surface plasmon resonance
- Toxin