Peptide-polymer bioconjugates combine oligopeptides with synthetic polymer blocks and can be used for various applications in material sciences. In recent years, bioconjugates were applied as compatibilizers and coatings.1,2 Biocombinatorial approaches, such as phage display, have been shown to yield strong binding peptides, which exhibit excellent coating properties as peptide-PEO conjugates.3 Phage display represents a widely exploited strategy to select peptides or proteins that exhibit highly specific affinity to various substrates.4 Following a phage display experiment, DNA sequencing of binding phage clones is required in order to get the sequence information of the binding peptides. Traditionally, random clone picking followed by Sanger sequencing was applied. However, this method may not necessarily identify the strongest binding clones. Next-generation sequencing made sequencing of whole phage libraries possible, which highly improved the selection of strong binders.5 Here, we show that the biocombinatorial method of phage display combined with next generation DNA sequencing of whole phage libraries represents a powerful tool for an application in material chemistry. Phage display is used to find specific target binding peptides for polypropylene surfaces (PP). PP binders are of particular interest because thus far gluing or printing on PP is challenging due to its low surface energy. Scripts for sequence data analysis were developed and promising sequences were synthesized as peptide-PEO conjugates. Fluorescence based adsorption experiments on PP surfaces led to the identification of strong binding sequences and a better understanding of the peptide-surface interactions. Figure. The concept of combining phage display with next-generation sequencing for the developement of adhesive peptide-polymer conjugates.

Biocombinatorially selected peptide-polymer conjugates as polypropylene binders

2019 Spring National Meeting

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