Voltammetric Detection of S100B Protein Using His-Tagged Receptor Domains for Advanced Glycation End Products (RAGE) Immobilized onto a Gold Electrode Surface.

Sensors (Basel, Switzerland)

PubMedID: 24940866

Mikula E, Wyslouch-Cieszynska A, Zhukova L, Puchalska M, Verwilst P, Dehaen W, Radecki J, Radecka H. Voltammetric Detection of S100B Protein Using His-Tagged Receptor Domains for Advanced Glycation End Products (RAGE) Immobilized onto a Gold Electrode Surface. Sensors (Basel). 2014;14(6):10650-63.
In this work we report on an electrochemical biosensor for the determination of the S100B protein. The His-tagged VC1 domains of Receptors for Advanced Glycation End (RAGE) products used as analytically active molecules were covalently immobilized on a monolayer of a thiol derivative of pentetic acid (DPTA) complex with Cu(II) deposited on a gold electrode surface. The recognition processes between the RAGE VC1 domain and the S100B protein results in changes in the redox activity of the DPTA-Cu(II) centres which were measured by Osteryoung square-wave voltammetry (OSWV). In order to verify whether the observed analytical signal originates from the recognition process between the His6-RAGE VC1 domains and the S100B protein, the electrode modified with the His6-RAGE C2 and His6-RAGE VC1 deleted domains which have no ability to bind S100B peptides were applied. The proposed biosensor was quite sensitive, with a detection limit of 0.52 pM recorded in the buffer solution. The presence of diluted human plasma and 10 nM Aß1-40 have no influence on the biosensor performance.