Modular Design for Proteins Assembling into Antifouling Coatings: Case of Gold Surfaces

We analyze modularity for a triblock protein designed to self-assemble into antifouling coatings. Previously, we have shown that the design performs well on silica surfaces when is taken to be a silica-binding peptide, is a thermostable trimer domain, and is the uncharged elastin-like polypeptide (ELP), = (GSGVP)₄₀. Here, we demonstrate that we can modulate the nature of the substrate on which the coatings form by choosing different solid-binding peptides as binding domain and that we can modulate antifouling properties by choosing a different hydrophilic block . Specifically, to arrive at antifouling coatings for gold surfaces, as binding block we use the gold-binding peptide GBP1 (with the sequence MHGKTQATSGTIQS), while we replace the antifouling blocks by zwitterionic ELPs of different lengths, = (GDGVP-GKGVP), with n = 20, 40, or 80. We find that even the proteins with the shortest blocks make coatings on gold surfaces with excellent antifouling against 1% human serum (HS) and reasonable antifouling against 10% HS. This suggests that the -- triblock protein can be easily adapted to form antifouling coatings on any substrate for which solid-binding peptide sequences are available.