Fusion　inhibitors　of　HIV　prevent　the　virus　from　entering　into　the　target　cell　via　the　interaction　with　gp41,　which　stops　the　process　of　spatial　rearrangement　of　the　viral　envelope　protein.　A　series　of　peptides　have　been　designed　and　screened　to　obtain　a　highly　potent　novel　sequence.　Among　them,　CT105　possesses　the　most　potent　anti-viral　ability　at　low　nanomolar　IC50　values　against　a　panel　of　HIV-1　pseudoviruses　from　A,　B,　C　and　A(1)/D　subtypes,　whereas　T20　shows　much　weaker　potency.　CT105　also　shows　excellent　inhibitory　activity　at　260　pico　molar　IC50　against　HIV-1　replication.　As　a　fusion　inhibitor,　CT105　has　a　strong　ability　to　interrupt　gp41　core　formation.　The　terminal　half-life　of　CT105　possesses　1.72-fold　longer　than　that　of　T20　as　determined　by　developing　an　indirect　competitive　ELISA　method.　The　results　suggest　that　this　artificial　peptide　CT105　could　be　a　favorable　architype　for　further　optimization　and　modification.　(C)　2018　Elsevier　Ltd.　All　rights　reserved.