Despite　the　synthetic　peptides　inhibit　HIV-1　entry;　its　application　of　this　peptide　therapy　may　be　limited　due　to　the　high　cost　of　the　peptide　production　and　lack　of　its　oral　availability.　Thus,　it　is　necessary　to　identify　the　small　molecule　inhibitors　reacting　with　the　same　or　overlapping　target　sites　on　gp41　recognizing　the　antiviral　peptides.　In　this　work,　a　small　inhibitor　(TP1)　is　docked　into　the　hydrophobic　grooves　of　gp41　by　using　AutoDock　software,　resulting　in　five　alternative　energetically　favorable　models.　The　data　from　other　studies　were　used　to　define　our　preferred　models.　We　found　that　only　one　binding　mode　is　supported　by　the　experimental　evidence.　The　model　could　be　used　to　design　more　effective　HIV-1　inhibitors　targeted　to　the　HIV-1　gp41　core　structure.　©　2005　IEEE.