Both PP1 and PP5 modified surfaces exhibit minimal affinity towards DNA origami, while these two surfaces are the most and the least hydrophilic (water contact angle: (38.9 ± 0.7)° vs. (69.2 ± 0.1)°) among the five polypeptoid brush monolayer modified surfaces. PP3 and PP4 with a high aromatic monomer composition (75% and 100%, respectively) enable preferential attachment of DNA origami on surfaces, with a much higher density as compared to the commonly used activated Si substrates under the same deposition conditions (Supporting Information, Figure ). Specific binding of biomolecules. Specific protein binding events typically involve biomolecular recognition between specific chemical groups and the protein. Here we show that as a surface modification material, functionalized polypeptoid brushes enable specific binding of proteins with a demonstration based on biotin-streptavidin interactions. PP1 is first identified to generate modified surfaces with minimal non-specific binding of streptavidin (Supporting Information, Figure ). This is within expectation as polypeptoid brushes with methoxyethyl side chains have been reported in multiple studies for creating antifouling surfaces against lysozyme, fibrinogen