Résumé
The reversible oriented immobilization of proteins on solid surfaces is a prerequisite for the investigationof molecular interactions at interfaces or the construction of supramolecular assemblies. We demonstratea generally applicable method using a synthetic chelator thioalkane which can self-assemble on a goldsurface via its thiol group. It exposes its nitrilotriacetic acid group which serves as a chelator fortransition metal ions. Reversible binding of a Fat, fragment modified with a C-terminal hexahistidineextension was monitored in situ using surface plasmon resonance. The directed immobilization ofproteins on surfaces opens new ways for structural investigations of proteins and the development ofbiosensors.