Integration is a critical step in the retroviral life cycle. HIV-1 integrase is involved in the integration of HIV DNA into host chromosomal DNA and appears to have no functionally equivalent in human cells. It has become an attractive and rational target for selective anti-AIDS therapy. A random linear heptapeptides phage display library was panned on the recombinant HIV-1 integrase protein. After five rounds of panning, 13 positive phage clones were selected and sequenced. Two consensus peptides (TPSHSSR and HPERATL) were chemically synthesized. The non-radioactive ELISA-based HIV-1 integrase assay showed that the synthetic peptides TPSHSSR and HPERATL were able to inhibit the 3'cleavage or strand transfer activity of HIV-1 integrase to some extent (IC₅₀=(54.56±5.18) μmol/L, IC₅₀=(28.29±1.32) μmol/L, respectively). These heptapeptides could be used for developing new anti-HIV drug candidates, as well as for structural studies of the three-dimensional structure of the entire integrase molecule.