Nine　bradykinin-related　peptides　were　identified　in　Phyllomedusa　sauvagei　skin　secretion　using　QTOF　MS/MS　fragmentation　sequencing.　The　major　peptides　were　(Thr(6))-bradykinin,　(Hyp(3),　Thr(6))-bradykinin,　(Thr(6))-phyllokinin　and　(Hyp(3),　Thr(6))-phyllokinin.　The　phyllokinins　occurred　in　both　sulfated　and　non-sulfated　forms.　All　(Thr(6))-substituted　bradykinins/phyllokinins　could　be　generated　from　a　common　precursor　by　differential　post-translational　processing　and　modification.　The　open-reading　frame　of　the　cloned　precursor　cDNA　consisted　of　62　amino　acid　residues　with　a　single　bradykinin/phyllokinin　coding　sequence　located　at　the　C-terminus.　Structural　features　included　a　Glu-Arg　processing　site　at　the　N-terminus　of　the　bradykinin/phyllokinin　domain　and　the　absence　of　an　acidic　amino　acid　residue　adjacent　to　the　C-terminal　Tyr　residue　in　the　phyllokinins.　However,　the　neutral　amino　acid　residue　(Ile)　at　position　-1　and　the　basic　amino　acid　residue　(Arg)　at　position　-2　from　the　Tyr　residue,　constitute　a　sulfation　motif　previously　identified　only　in　a　protochordean.　(C)　2003　Elsevier　Inc.　All　rights　reserved.