The　recognitions　and　interactions　of　a　series　of　aryl　diketoacid　(ADK)　inhibitors　with　HIV-1　integrase　(IN)　were　studied　via　molecular　docking　method.　The　results　indicate　that　the　inhibitors　bind　to　the　pocket　(formed　by　Asp64　similar　to　Leu68,　Thr115　similar　to　Phe121,　Gln148　similar　to　Lys159　and　Mg2+　ion)　of　IN,　and　the　inhibiting　mechanism　is　similar　to　that　of　5CITEP.　Molecular　dynamics　simulation　and　MM/PBSA　methods　were　used　to　calculate　the　binding　free　energy　between　ADK　inhibitors　and　IN.　The　calculated　binding　free　energy　agrees　well　with　experimental　data,　and　the　average　absolute　deviation　is　3.6　kJ/mol.　It　was　also　found　that　the　formation　of　the　complex　was　mainly　driven　by　the　favorable　van　der　Waals＇(VDW)　interactions　in　the　system　and　the　favorable　non-polar　item　of　the　solvent　effect.　Correlation　analysis　shows　that　the　binding　free　energy　has　obvious　linear　correlation　with　the　hydrophobic　interaction　(R=0.61),　from　which　a　good　model　predicting　the　binding　free　energy　of　ADK　inhibitors　with　HIV-1　IN　has　been　obtained　through　a　multiple　linear　regression　method.　All　the　above　simulation　results　provide　us　with　some　helpful　instruction　for　the　anti-HIV　drug　design　based　on　the　structures　of　inhibitors.