We analyze modularity for aB-M-Etriblock protein designed to self-assemble into antifouling
coatings.
Previously, we have shown that the design performs well on silica
surfaces whenBis taken to be a silica-binding
peptide,Mis a thermostable trimer
domain, andEis 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 domainBand that we can
modulate antifouling properties by choosing a different hydrophilic
blockE. Specifically, to arrive at
antifouling coatings for gold surfaces, as binding blockBwe use the gold-binding peptide GBP1 (with the
sequence MHGKTQATSGTIQS), while we replace the antifouling blocksEby zwitterionic ELPs of different lengths,EZn= (GDGVP-GKGVP)n/2,
withn= 20, 40, or 80. We find that even theB-M-Eproteins with the shortestEblocks make coatings on gold surfaces with excellent
antifouling against 1% human serum (HS) and reasonable antifouling
against 10% HS. This suggests that theB-M-Etriblock
protein can be easily adapted to form antifouling coatings on any
substrate for which solid-binding peptide sequences are available.