Interaction of Cationic Polypeptides with ElectroactivePolypyrrole/Poly(Styrenesulfonate) and Poly(N-Methylpyrrole)/Poly(Styrenesulfonate) Films

摘要

The binding of cationic polypeptides to polypyrrole PP/poly(styrenesulfonate)PSSand poly(N-methylpyrrole) PNMP/pss films, along with the effect of binding on film electroactivity, have been studied using the electrochemical quartz-crystal microbalance (EQCM). Two polypeptides were studied, namely poly(l-lysine hydrochloride) and the arginine-rich histone H3. Poly(l-lysine hydrochloride) binds to either the oxidized or reduced forms of the films, although the electroactivity and ability of the films to transport small cations upon electrochemical cycling remains intact. Histone H3 shows little tendency to bind to oxidized films, but upon electrochemical reduction PSS is extracted. This unusual behavior is thought to be the result of strong electrostatic and hydrophobic interactions between PSS and H3 at the PP/PSS surface. The films retain their electroactivity after interaction with H3.