The ability to control of interfacial interactions is important for the efficacy of drug/gene delivery, the protection of therapeutic proteins, the performance of surface-based diagnostic devices and the bio-compatibility of implantable materials. It is particularly tricky to develop non-fouling materials that can preserve the bioactivity of proteins at the same time. The novelty of the proposed research is focused on non-fouling, enzyme stabilizing interfacial interactions of naturally occurring poly-zwitterions and proteins. This proposal seeks to address critical structure-property relations, e.g. ion separation distances, hydration and counter-charge distibution and their relation to enzyme stability. If successful, such a broader understanding of zwitterionic materials could provide guidance towards novel building blocks for better multifunctional materials, and could have impact on the field of biomaterials and biointerfaces.
