Screening Methods for Hydrophobins and Peptides as Potential Promoters of Polymer Adhesion

Bacterial cell surface display libraries have been adapted to identify potentially promising proteins and peptides with adhesive characteristics against an array of diverse substrates. The peptide display libraries were screened using methods previously developed by the Army Research Laboratory to find promising peptide sequences that interacted strongly with substrates such as gold or ITO nanoparticles. The current work combines peptide display with microfluidic approaches to screen material substrates (e.g. polymers, metals) that may exhibit weaker interactions than those probed previously. In addition to the display of a peptide library, a class of natural surfactants known as hydrophobins have been expressed on the bacteria surface. Hydrophobins are used by fungi to breach air-water interfaces when colonizing new environments, and have already been shown to adhere to highly non-polar surfaces, such as Teflon or polystyrene.<br/>Progress towards identifying proteins and peptides that promote bacterial adhesion to diverse polymer substrates and demonstration of microfluidic-based methods for obtaining semi-quantitative data on binding affinity with reasonable throughput will be discussed. This work will ultimately merge the screening tools of synthetic biology approaches to address long-standing challenges in materials science, providing new insights for probing adhesion.