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.
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.
Thompson
Alan Hunter
AH
Institute of Biomedical Sciences, University of Ulster, Coleraine, Co Londonderry BT52 1SA, UK.
Bjourson
Anthony John
AJ
Orr
David Francis
DF
Shaw
Chris
C
McClean
Stephen
S
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
D029845:Amphibian Proteins; D018076:DNA, Complementary; D009479:Neuropeptides; D010455:Peptides; C045322:phyllomedusin