The　binding　mode　of　a　series　of　dicaffeoyl　or　digalloyl　pyrrolidine　and　furan　derivatives　inhibitors　with　HIV-1　integrase　was　proposed　by　using　molecular　docking　and　molecular　dynamics　(MD)　simulation　methods.　The　results　indicate　that　the　interactions　between　HIV-1　integrase　conserved　DDE　motif　and　caffeoyl　or　galloyl　group　of　inhibitors　play　a　critical　role　in　the　inhibition　of　integrase　activity,　and　the　binding　affinity　between　integrase　and　inhibitors　was　improved　when　the　side　chain　groups　were　galloyls.　The　linear　interaction　energy　(LIE)　method　was　used　to　calculate　the　binding　free　energies　of　HIV-1　integrase　and　their　inhibitors,　the　predicted　values　are　in　good　agreement　with　the　experimental　data,　with　a　root-mean-square　deviation　(RMSD)　of　1.39　kJ.mol(-1).　The　above　results　provide　useful　information　for　structure-based　HIV-1　integrase　inhibitor　design.