Glycoprotein assay based on the optimized immittance signal of a redox tagged and lectin-based receptive interface.

摘要: Abstract Glycoproteins play important roles in biological systems such as process related to cell binding, signaling and disease. Consequently, novel, potentially quantitative, rapid electroanalytical approaches capable of detecting protein binding are welcome. Herein, we introduce a methodology that is both fast sensitive, quantification the affinity glycoprotein-lectin molecular models. The proposed based on electrochemical impedance spectroscopy technique focused immittance function approach, wherein library analytical parameters can be computed from raw data obtained, automatically processed label-free, quantifiable very sensitive assay platform. This approach also avoids redox probe pre-doping sample. Avoiding sample achievable designing an appropriate redox-tagging monolayer containing lectin interface (a carbohydrate protein, herein ArtinM) bio-receptor, endowing high sensitivity signal when specifically glycoproteins interest (presently horseradish peroxidase, HRP, mannose glycoprotein) biochemical target for ArtinM. curves demonstrated constant could evaluated equivalent all (immittance function) parameters, allowing optimized single frequency (or range frequencies) assessment with sensitivity. In other words, constants between ArtinM HRP each at given frequencies were similar, independently parameter. Thus, feasibility using this glycoarrays by accessing bio-recognition processes (optimized) highly multiplexable platform was demonstrated.