Modular Design for Proteins Assembling into Antifouling Coatings: Case of Gold Surfaces
Chuanbao Zheng, Nicolò Alvisi, Robbert Jan de Haas, Zhisen Zhang, Han Zuilhof, Renko de Vries
Abstract
High Resolution Image Download MS PowerPoint Slide We analyze modularity for a B-M-E triblock protein designed to self-assemble into antifouling coatings. Previously, we have shown that the design performs well on silica surfaces when B is taken to be a silica-binding peptide, M is a thermostable trimer domain, and E is the uncharged elastin-like polypeptide (ELP), E = (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 B and that we can modulate antifouling properties by choosing a different hydrophilic block E . Specifically, to arrive at antifouling coatings for gold surfaces, as binding block B we use the gold-binding peptide GBP1 (with the sequence MHGKTQATSGTIQS), while we replace the antifouling blocks E by zwitterionic ELPs of different lengths, E Z n = (GDGVP-GKGVP) n /2, with n = 20, 40, or 80. We find that even the B-M-E proteins with the shortest E blocks make coatings on gold surfaces with excellent antifouling against 1% human serum (HS) and reasonable antifouling against 10% HS. This suggests that the B - M - E triblock protein can be easily adapted to form antifouling coatings on any substrate for which solid-binding peptide sequences are available.