The low surface energies of hydrophobic polymers such as polystyrene make it difficult to promote adhesion to these substrates without chemical or physical pre-treatment. This reduces the ability to conduct repairs of these materials at the point of need, limits their application, and can cause difficulties in 3D printing. In nature, peptides have evolved to fit many organismal needs such as structural, signaling, and antimicrobial functions. Screening a large library of peptides for binding affinity is attractive as the set of canonical amino acids shows wide functional diversity, and it is possible to precisely alter that functionality when the peptide is biologically synthesized. Given a large-enough compositional space, there is likely to be a peptide which binds to a hydrophobic polymer, and such a peptide can be used to provide mechanistic insights for how binding to these difficult substrates may be achieved.<br/><br/>In this work, a library of approximately 250,000 peptides was displayed on the surface of <i>Escherichia coli</i>, and this library was screened for promoting bacterial adhesion to polystyrene and acrylic. Next-generation sequencing was used to determine the ten most prevalent peptides after four rounds of washing. The adhesion-promoting characteristics of these most-prevalent peptides were then ranked in a semi-quantitative manner using a commercially-available microfluidic chip, and a new microfluidic chip of our own design. Candidate peptides were then systematically mutated to probe which amino acids were critical to the binding function of the peptide. These results are being used to draw insights into binding mechanisms that will eventually assist in modelling the peptide’s behavior at a substrate interface, leading to improved understanding for the design of new adhesives. Sequence information is being analyzed in the context of specific peptide-substrate interactions as well as gross polar-non-polar interactions and Hansen Solubility parameters.

Insights into binding hydrophobic polymers from peptide screening and mutagenesis

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