Characterization and applications of affinity based surface modification of polypyrrole

I present the characterization and applications of a technique to modify the surface of the conducting polymer, polypyrrole, via a novel, 12-amino acid peptide, THRTSTLDYFVI (T59). This peptide non-covalently binds to the chlorine-doped conducting polymer polypyrrole, allowing it to be used in tethering molecules to polypyrrole for uses such as a scaffold for the treatment of peripheral nerve injury or in surface coatings of neural recording electrodes. I have quantified the binding of this peptide as well as investigating the mechanism of the binding. The equilibrium constant of the binding interaction of PPyCl and the T59 peptide was found through a binding assay to be 92.6 nM, and the off rate was found to be approximately 2.49 s⁻¹, via AFM force spectroscopy. The maximum observed surface density of the peptide was 1.27 +/- 0.42 femtomoles/cm². Furthermore, my studies suggest that the eighth residue, aspartic acid, is the main contributor of the binding, by interacting with the partially positive charge on the backbone of polypyrrole. I have demonstrated practical applications of the technique in the successful modification of a PPyCl surface with the laminin fragment IKVAV, as well as the so-called stealth molecule poly(ethylene glycol) (PEG). A subcutaneous implant study was performed to confirm that the T59 peptide did not induce any significant reaction in vivo. Significantly, the conductivity of a PPyCl surface was unaffected by this surface modification technique.