Many materials are used during a dental treatment, which can cause dental allergy in susceptible patients. Behind the immune response there are multistage biochemical processes, in which protein interactions can be investigated by directed evolutionary, phage display technique. Aim of this study is to determine the frequent amino acid sequences on polystyrene surface as dental base thermoplastic polymers by phage display technique. Positive control was streptavidin (Str) covered polymer, the negative control was bovine serum albumin blocked polystyrene. Based on our results it was found that the WLFNHPQ sequence is Str specific peptide in our system, because this variant has occurred repeatedly in three independent samples. The selected phages from the BSA blocked PS surface have contained some variants with some frequency. We demonstrated that peptides bond to PS surface. The most frequent peptide was FSGRPLP on untreated polystyrene surface. However allergy is not reported with the application of PS thermoplastic polymer. The reason of this can be the result of the applied technology, namely the injection moulded technique. In the antigen presentation the knowledge and blocking of the binding sites can help to discover and reduce the formation of allergic reactions. Based on our experiments it can be declared that our PS model system can be a good starting point in the recognition of other dental polymer peptide biding sites.