Dynamic Control of Protein-Protein Interactions

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• 作者：Megan L. O'Grady ; Kevin Kit Parker
• 刊名：Langmuir
• 出版年：2008
• 出版时间：January 1, 2008
• 年：2008
• 卷：24
• 期：1
• 页码：316 - 322
• 全文大小：213K
• 年卷期：v.24,no.1(January 1, 2008)
• ISSN：1520-5827

文摘

The capability to selectively and reversibly control protein-protein interactions in antibody-doped polypyrrole(PPy) was accomplished by changing the voltage applied to the polymer. Polypyrrole was doped with sulfate polyanionsand monoclonal anti-human fibronectin antibodies (FN). The ability to toggle the binding and dissociation of fibronectin(FN) to FN-doped polypyrrole was demonstrated. Staircase potential electrochemical impedance spectroscopy (SPEIS)was performed to characterize the impedance and charge transfer characteristics of the FN-doped PPy as a functionof applied voltage, frequency, and FN concentration. Impedance measurements indicated oxidation of FN-dopedPPy promoted selective binding of FN to FN antibodies and reduction of the polymer films facilitated FN dissociation.Moreover, SPEIS measurements suggested that the apparent reversibility of antigen binding to antibody-doped PPyis not due to the suppression of hydrophobic binding forces between antibody and antigen. Instead, our data indicatethat reversible antigen binding to antibody-doped PPy can be attributed to the minimization of charge in the polymerfilms during oxidation and reduction. Furthermore, FN-doped PPy was utilized to collect real-time, dynamicmeasurements of varying FN concentrations in solution by repeatedly binding and releasing FN. Our data demonstratethat antibody-doped PPy represents an electrically controllable sensing platform which can be exploited to collectrapid, repeated measurements of protein concentrations with molecular specificity.