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    Design of Polypeptides Self-Assembling into Antifouling Coatings: Exploiting Multivalency

    Journal: Biomacromolecules, Volume 23, SEP 12

    Authors: Alvisi, Nicolo; Zheng, Chuanbao; Lokker, Meike; Boekestein, Victor; de Haas, Robbert; Albada, Bauke; de Vries, Renko

    Organizations: NWO-TTW-OTP [15481]; VLAG Graduate School; China Scholarship Council

    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 recombi n a n t production is low. For a si n g l e design, with the domain structure B- M-E, both solubi l i t y 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. Gi v e n 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.
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