HIV-1　integrase(IN)　plays　a　crucial　role　in　the　retroviral　life　cycle.　The　peptides　derived　from　the　helix　of　IN　were　reported　to　have　the　potency　of　inhibition.　We　designed　a　series　of　peptides　based　on　interface　helices　alpha　1　and　alpha　5　with　the　aim　of　increasing　their　inhibitory　activity.　The　helix-forming　tendency　and　the　affinity　with　IN　were　essential　for　interfacial　peptide　inhibitors.　The　MD　simulation　and　AGADIR　prediction　both　showed　favorable　results　for　the　designed　peptides.　The　binding　mode　and　binding　free　energy　of　peptide　and　IN　were　investigated　subsequently　to　test　our　design.　The　improvement　in　binding　free　energy　compared　with　that　of　alpha　1　and　alpha　5　indicates　that　some　of　the　designed　peptides　may　have　a　higher　potency　for　inhibiting　the　dimerization　of　IN.　This　study　provides　some　useful　information　for　rational　design　of　IN　peptide　inhibitor.