We demonstrated the selection and characterization of polymer-binding peptides, and their application as surface modifiers. Peptides that bind specifically to polyetherimide (PEI) films were successfully identified from a phage-displayed peptide library. A chemically-synthesized peptide with the sequence of Thr-Gly-Ala-Asp-Leu-Asn-Thr (p1) showed high affinity toward PEI films (5.6×10⁸ M^-1). The peptide was biotinylated and immobilized onto the PEI films to function as a linker for the subsequent immobilization of streptavidin (SAv). We found that several factors could significantly affect the amount of SAv bound. Furthermore, we demonstrated that the SAv immobilized onto the PEI films via the biotinylated peptides was uniformly distributed, and thus was able to further immobilize probe DNA and to observe hybridization with complementary DNA. The present study offered new and significant insights into the modification of polymer film surfaces with specific binding peptides.