Peptidomic analysis (reversed-phase HPLC combined with MALDI-TOF mass spectrometry and automated Edman degradation) of norepinephrine-stimulated skin secretions from the Trinidadian leaf frog Phyllomedusa trinitatis Mertens 1926 led to the identification and structural characterization of 26 host-defense peptides. On the basis of amino acid sequence similarity, the peptides may be divided into the followings groups: dermaseptins with the conserved N-terminal region GLWSKIK (6 peptides), dermaseptins with the N-terminal region ALWKXXLK (5 peptides) dermaseptins with the conserved N-terminal region GLFKTLIKGAGKMLGHVAK (4 peptides), C-terminally α-amidated and non-amidated forms of the phylloseptins (9 peptides), phyllocaerulein, a peptide (GLVSGLLNSVTGLLGN LAGGGL) with structural similarity to the plasticins, and a putative antioxidant peptide (LTWKIPTRFCGVT). The primary structures of the peptides support the claim based upon morphological criteria that P. trinitatis and Phyllomedusa tarsius are very closely related phylogenetically but are probably not conspecific.
|Journal||Comparative Biochemistry and Physiology - Part D: Genomics and Proteomics|
|Early online date||30 Jun 2018|
|Publication status||E-pub ahead of print - 30 Jun 2018|
- host-defense peptide
- antioxidant peptide
- frog skin