Electropolymerization of a phenol-modified peptide for use in receptor-ligand interactions studied by surface plasmon resonance.
The combination of surface plasmon resonance (SPR) with an electrochemical method for surface modification is presented. The SLP1 sequence of the sodium channel protein of rat cardiac muscle cells was N-terminally modified with an electropolymerizable group and immobilized on a gold-coated glass slide by oxidative polymerization. The resulting peptide-functionalized substrate was incubated with a polyclonal-specific anti-SLP1 serum. Growth of the peptide layer and the immunological reaction between ligand and receptor were detected on-line by SPR. The applicability of this approach for the rapid and selective analysis of receptor-ligand interactions is demonstrated.
Kienle
S
S
Institut für Organische Chemie, Universität Tübingen, Germany.
Lingler
S
S
Kraas
W
W
Offenhäusser
A
A
Knoll
W
W
Jung
G
G
D000595:Amino Acid Sequence; D000818:Animals; D015374:Biosensing Techniques; D008024:Ligands; D008969:Molecular Sequence Data; D009206:Myocardium / Q000378:metabolism*; D010455:Peptides; D019800:Phenol; D051381:Rats; D011956:Receptors, Cell Surface / Q000032:analysis* / Q000378:metabolism; D015222:Sodium Channels / Q000032:analysis* / Q000378:metabolism
D008024:Ligands; D010455:Peptides; D011956:Receptors, Cell Surface; D015222:Sodium Channels; D019800:Phenol