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The affinity of surfaces toward proteins is found to be a key parameter to govern the synthesis of polymer brushes by surface-initiated biocatalytic atom transfer radical polymerization (SI-bioATRP). While the "ATRPase" hemoglobin (Hb) stimulates only a relatively slow growth of protein repellent brushes, the synthesis of thermoresponsive grafts can be regulated by switching the polymer's attraction toward proteins across its lower critical solution temperature (LCST). Poly(N-isopropylacrylamide) (PNIPAM) brushes are synthesized in discrete steps of thickness at temperatures above LCST, while the biocatalyst layer is refreshed at T &lt; LCST. Multistep surface-initiated biocatalytic ATRP demonstrates a high degree of control, results in high chain end group fidelity and enables the synthesis of multiblock copolymer brushes under fully aqueous conditions. The activity of Hb can be further modulated by tuning the accessibility of the heme pocket within the protein. Hence, the multistep polymerization is accelerated at acid pH, where the enzyme undergoes a transition from its native to a molten globule conformation. The controlled synthesis of polymer brushes by multistep SI-bioATRP highlights how a biocatalytic synthesis of grafted polymer films can be precisely controlled through the modulation of the polymer's interfacial physicochemical properties, in particular of the affinity of the surface toward proteins. This is not only of importance to gain a predictive understanding of surface-confined enzymatic polymerizations, but also represents a new way to translate bioadhesion into a controlled functionalization of materials.

Controlling Enzymatic Polymerization from Surfaces with Switchable Bioaffinity