title: Amphibian skin secretomics: application of parallel quadrupole time-of-flight mass spectrometry and peptide precursor cDNA cloning to rapidly characterize the skin secretory peptidome of Phyllomedusa hypochondrialis azurea: discovery of a novel peptide family, the hyposins.
abstract: This study reports the variety of peptides present in the skin secretory peptidome of Phyllomedusa hypochondrialis azurea. Peptide structures, along with post-translational modifications, were elucidated by QTOF MS/MS analysis, cDNA sequencing, or a combination of both. Twenty-two peptides, including 19 novel structures, were identified from six different structural classes, including tryptophyllins, dermorphins, and a novel group of peptides termed hyposins. The study demonstrates the power of this combined approach to mine the rich peptidome compliment of the amphibian defensive skin secretome.
authors: Institute of Biomedical Sciences, University of Ulster, Coleraine, Co Londonderry BT52 1SA, UK.
authors: Alan Hunter
authors: AH
authors: Thompson
authors: Anthony John
authors: AJ
authors: Bjourson
authors: David Francis
authors: DF
authors: Orr
authors: Chris
authors: C
authors: Shaw
authors: Stephen
authors: S
authors: McClean
mesh_terms: D000595:Amino Acid Sequence; D029845:Amphibian Proteins / Q000737:chemistry; D000663:Amphibians; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000378:metabolism; D008969:Molecular Sequence Data; D009479:Neuropeptides / Q000378:metabolism*; D010455:Peptides / Q000737:chemistry; D040901:Proteomics / Q000379:methods*; D012689:Sequence Homology, Nucleic Acid; D012867:Skin / Q000378:metabolism*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
chemical_list: D029845:Amphibian Proteins; D018076:DNA, Complementary; D009479:Neuropeptides; D010455:Peptides; C045322:phyllomedusin