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

ABSTRACT: 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<

SUBMITTER: Alvisi N 

PROVIDER: S-EPMC9472226 | biostudies-literature | 2022 Sep

REPOSITORIES: biostudies-literature