Bradykinin-related　peptides　(BRPs)　represent　one　of　the　most　widespread　and　closely　studied　families　of　amphibian　defensive　skin　secretion　peptides.　Apart　from　canonical　bradykinin　(RPPGFSPFR)　that　was　first　reported　in　skin　extracts　of　the　European　brown　frog,　Rana　temporatia,　many　additional　site-substituted,　N-　and/or　C-terminally　extended　peptides　have　been　isolated　from　skin　extracts　and　secretions　from　representative　species　of　the　families　Ranidae,　Hylidae,　Bombinatoridae　and　Leiopelmatidae.　The　most　diverse　range　of　BRPs　has　been　found　in　ranid　frog　skin　secretions　and　this　probably　reflects　the　diversity　and　number　of　species　studied　and　their　associated　life　histories　within　this　taxon.　Amolops　(torrent　or　cascade　frogs)　is　a　genus　within　the　Ranidae　that　has　been　poorly　studied.　Here　we　report　the　presence　of　two　novel　BRPs　in　the　skin　secretions　of　the　Chinese　Wuyi　Mountain　torrent　frog　(Amolops　wuyiensis).　Amolopkinins　W1　and　W2　are　dodecapeptides　differing　in　only　one　amino　acid　residue　at　position　2　(Val/Ala)　that　are　essentially　(Leu(1),　Thr(6))-bradykinins　extended　at　the　N-terminus　by　either　RVAL　(W1)　or　RAAL　(W2).　Amolopkinins　W1　and　W2　are　structurally　similar　to　amolopkinin　L1　from　Amolops　loloensis　and　the　major　BRP　(Leu(1),　Thr(6),　Trp(8))-bradykinin　from　the　skin　of　the　Japanese　frog,　Rana　sakuraii.　A.　wuyiensis　amolopkinins　were　separately　encoded　as　single　copies　within　discrete　precursors　of　61　amino　acid　residues　as　deduced　from　cloned　skin　cDNA.　Synthetic　replicates　of　both　peptides　were　found　to　potently　antagonize　the　contractile　effects　of　canonical　bradykinin　on　isolated　rat　ileum　smooth　muscle　preparations.　Amolopkinins　thus　appear　to　represent　a　novel　sub-family　of　ranid　frog　skin　secretion　BRPs.　(C)　2009　Elsevier　Inc.　All　rights　reserved.