Abstract: Objective To screen and characterize the short peptides which bind specifically to interleukin-2 (IL-2) receptor α chain (IL-2Rα) for acquisition of small antagonists for blocking the binding of IL-2 with IL-2Rα. Methods 12-mer phage displayed peptide library was screened with the target cells of MT-2 cells which expressed IL-2Rα at high levels. The binding phage clones were eluted by anti-IL-2Rα monoclonal antibody. After 3 rounds of screening, the positive phage clones were identified by enzyme-linked immunosorbent assay (ELISA) and immunohistochemistry, and the amino acid sequences of the positive clones were deduced from the DNA sequences. Results Seven positive clones were screened out of the 17 phage clones bound to MT-2 cells. The positive clone M15 could bind specifically to MT-2 cell and PHA-activated peripheral blood monouclear cells. Amino acid sequence analysis identified 6 sequences, all of which contained hydrophilic residues, and 5 of these 6 sequences included Tyr, Phe and Leu conservative residues. Conclusion The peptide sequences containing Tyr, Phe conservative residues identified in this study can bind to cell surface IL-2Rα.