Objective   To screen specific binding peptide of integrin αvβ3 using phage display random peptide library technology and analyze the function of potential peptide.    Methods   Five short peptides designed according to the crystal structure of the extracellular segment and protein sequence of integrin αvβ3 were utilized as selected ligands and coded from 1 to 5. After 3 rounds of screening

positive phage clones were identified by sandwich ELISA and DNA sequencing. Functions of the peptides were further identified with adhesion test.    Results   After 3 rounds of screening

the enriched phage clones were identified. As a representative

7 of 12 phage clones were identified positive by ELISA

which had comparatively strong binding activity to synthesized peptide coded 5. Two sequences were obtained

and the consensus sequence was ****HRH and HWR****. Adhesion test showed that chemical synthesized peptides “FITC-HLPWHRH，FITC-HWRLHPH” had higher binding affinities to M2 cells expressing integrin αvβ3.    Conclusion   The peptides with high affinity to integrin αvβ3 can be obtained through the screening of phage random peptide library with the synthesized peptides in vitro

which is beneficial to the further studies on the function of integrin αvβ3 in the early diagnosis of cancer and targeting angiogenesis inhibitors specific drug design.