To screen and identify the short peptides with specific binding activity to human CDS9 and to design the short-peptide clamp against tumor escape, the phage display peptide library containing 12 peptides was used to select the highly expressed specific coalescent peptide of human CD59 in CHO cells. Positive phage clones obtained after 5 rounds of biopanning and detected with ELISA were obtained , in which 8 of them with high binding activity to human CD59 were sequenced. The 3 sequences thus obtained showed high homology with each and certain homology with sequence with human CD2 (PubMed 339HGAAENSISPSS), and all contained primary structure HXAXXXXXXPXX, of which this sequence may be the mimic conformational epitope binding to human CD59. These results in the present study may be helpful to design the short-peptide clamp against the active sites of CD59 on tumor escape. To screen and identify the short peptides with specific binding activity to human CDS9 and to design the short-peptide clamp against tumor escape, the phage display peptide library containing 12 peptides was used to select the highly expressed specific coalescent peptide of human CD59 in CHO cells The 3 sequence was obtained showed high homology with each and certain homology with sequence with human CD2 (PubMed 339 HGAAENSISPSS), and all contained primary structure HXAXXXXXXPXX, of which this sequence may be the mimic conformational epitope binding to human CD59. These results in the present study may be helpful to design the short-peptide clamp against the active sites of CD59 on tumor escape.