The performance of synthetic polymer membranes when filtering bioprocessing fluids is severely limited by the interaction of proteins with the surface of the membranes. Synthesizing membranes with polymers that reduce such interactions has resulted in improved filtration performance. Our efforts to develop and test protein adhesion-resistant membranes and to determine protein-substrate adhesion, protein conformational stability, and protein aggregation at interfaces directly address this limitation. We have made significant progress in developing protein resistant membranes and in gaining fundamental insight into protein-polymer interactions. Heterogeneous and homogeneous surfaces that exhibit minimal adhesive energy and minimal amounts of protein adsorption have been identified. However, much work still needs to be done. In this presentation we summarize our most recent results on nature-inspired protein-resistant surfaces, on surfaces that can be triggered to change from polar to apolar, on protein-polymer interactions and on protein aggregation into amyloid fibrils.