Surface-bound polyelectrolyte structures are being designed for tunable protein uptake from solution. SPR measurements indicate at pH 6 poly(2-(dimethylamino)ethyl methacrylate) (PDMAEMA) brushes end-grafted from gold surfaces by atom transfer radical polymerization (ATRP) adsorb net-negatively charged bovine serum albumin (BSA) to an extent equivalent to 10 BSA monolayers. The adsorbed BSA mass per unit volume in the brush is comparable to its aqueous solubility limit in some cases. BSA uptake scales linearly with the surface concentration of grafted PDMAEMA, regardless of the degree of polymerization and grafting density for all brushes examined; BSA is bound at a constant ratio of 120 DMAEMA monomer units per BSA molecule. The adsorption is electrostatically driven. Desorption is possible only by manipulating the pH and/or ionic strength to weaken the electrostatic attraction. Net positively charged lysozyme is completely rejected by the brush. Quantitative structure-activity relationships between protein size and electrostatically driven uptake in PDMAEMA brushes will be discussed. If instead of a brush, a lightly crosslinked PDMAEMA hydrogel is attached to the surface, both the binding kinetics and the extent of BSA uptake are diminished. BSA binding occurs at > 1000 DMAEMA units per BSA. This is attributed to the inability of crosslinked PDMAEMA chains to adequately reconfigure to accommodate bound BSA. Lastly, current efforts to copolymerize PDMAEMA with more hydrophobic segments in order to achieve thermally programmable protein uptake will be described.