Abstract
The need to discover new peptide sequences to perform particular tasks has lead to a variety of peptide screening methods: phage display, yeast display, bacterial display and resin display. These are effective screening methods because the role of background binding is often insignificant. In the field of nonfouling materials, however, a premium is placed on chemistries that have extremely low levels of nonspecific binding. Due to the presence of background binding, it is not possible to use traditional peptide screening methods to select for nonfouling chemistries. Here, we developed a peptide screening method, as compared to traditional methods, that can successfully evaluate the effectiveness of nonfouling peptide sequences. We have tested the effect of different peptide lengths and chemistries on the adsorption of protein. The order of residues within a single sequence was also adjusted to determine the effect of charge segregation on protein adsorption.
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