We propose to exploit multivalent binding of solid-binding
peptides
(SBPs) for the physical attachment of antifouling polypeptide brushes
on solid surfaces. Using a silica-binding peptide as a model SBP,
we find that both tandem-repeated SBPs and SBPs repeated in branched
architectures implemented via a multimerization domain work very well
to improve the binding strength of polypeptide brushes, as compared
to earlier designs with a single SBP. At the same time, for many of
the designed sequences, either the solubility or the yield of recombinant
production is low. For a single design, with the domain structure
B
-
M
-
E
, both solubility and yield of recombinant production
were high. In this design,
B
is a silica-binding
peptide,
M
is a highly thermostable,
de novo-designed trimerization domain, and
E
is a hydrophilic elastin-like polypeptide. We show that the
B
-
M
-
E
triblock polypeptide rapidly assembles into highly
stable polypeptide brushes on silica surfaces, with excellent antifouling
properties against high concentrations of serum albumin. Given that
SBPs attaching to a wide range of materials have been identified,
the
B
-
M
-
E
triblock design provides a template
for the development of polypeptides for coating many other materials
such as metals or plastics.