Charge-driven and reversible assembly of ultra-dense polymer brushes: formation and antifouling properties of a zipper brush

Abstract

We investigated a new type of polymer brushes: the zipper brush. By adsorbing a diblock-copolymer with one charged block and one neutral block to an oppositely charged polyelectrolyte brush, a neutral polymer brush is formed on top of an almost neutral complex layer of polyelectrolytes. This neutral brush can be adsorbed in minutes and desorbed in seconds to restore the original polyelectrolyte brush. The zipper brush can be used, for example, as an antifouling layer to prevent protein adsorption. These characteristics are shown by fixed-angle optical reflectometry for the system of poly(N-methyl-2-vinyl pyridinium)-block-poly(ethylene oxide) (P2MVP-PEO) adsorbed to a poly(acrylic acid) (PAA) brush. After the diblock-copolymer has adsorbed (at pH 6), the charges of the PAA brush are almost completely compensated by the charges of the P2MVP block. The grafting density of the formed neutral brush can be controlled by the chain length and grafting density of the PAA brush, and by the chain length of P2MVP block. As the P2MVP blocks used in this study are much smaller than the PAA chains in the brush, the grafting density of the PEO brushes are found to be a multiplication of that of the PAA brush, and much higher grafting densities (up to 1.59 chains per nm²) can be obtained than previously reported for polymer brushes prepared by adsorption. At low pH, when the PAA is uncharged, only a few mg m⁻² adsorb probably because of hydrogen bonding between uncharged PAA and PEO. As the pH increases the PAA becomes more charged and the adsorbed amount of diblock-copolymer increases strongly until pH 6 and then levels off between pH 6 and pH 10. At pH 6 and 10 high salt concentrations (above 250 mM) are needed to significantly reduce the adsorbed amount. The antifouling properties of the zipper brush were tested by exposing the brush to a number of different protein solutions. For the proteins lysozyme, fibrinogen, bovine serum albumin, and b-lactoglobuline the zipper brush completely prevented any adsorption, for cytochrome C a small amount of adsorption was observed.