| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 740764 | Sensors and Actuators B: Chemical | 2011 | 6 Pages |
A surface plasmon resonance (SPR) sensor chip with immobilized protein G was used for simultaneously capturing, purifying and orienting antibody ligands. The ligands were further stabilized by chemical cross-linking. This procedure of designing the sensor chip improved efficient use of the ligands and could prolong the analytical use.The procedure was evaluated on standard dextran-coated sensor chips onto which commercial semi-purified antibodies towards human serum albumin and human troponin where captured and used for analysing their antigens.The procedure demonstrates a general design approach for presenting the biorecognition element on a biosensor surface which enhances sensitivity, stability and selectivity at the same time as an impure ligand is purified.
► Antibody ligands are oriented on surface plasmon resonance biochips by protein G. ► The biochips are used for assaying analytes to the oriented and bound antibodies. ► The chips are demonstrated on semi-purified antibodies towards albumin and troponin. ► The ligands can be chemically cross-linked prolonging their operational stability.
