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 electrochem ical method for surface modification is presented. The SLP1 sequence o f the sodium channel protein of rat cardiac muscle cells was N-termina lly modified with an electropolymerizable group and immobilized on a g old-coated glass slide by oxidative polymerization. The resulting pept ide-functionalized substrate was incubated with a polyclonal-specific anti-SLP1 serum. Growth of the peptide layer and the immunological rea ction between ligand and receptor were detected on-line by SPR. The ap plicability of this approach for the rapid and selective analysis of r eceptor-ligand interactions is demonstrated. (C) 1997 Elsevier Science Limited.