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The fallaxidin peptides from the skin secretion of the Eastern Dwarf Tree Frog Litoria fallax . Sequence determination by positive and negative ion electrospray mass spectrometry: antimicrobial activity and cDNA cloning of the fallaxidins
Author(s) -
Jackway Rebecca J.,
Bowie John H.,
Bilusich Daniel,
Musgrave Ian F.,
SurinyaJohnson Kathy H.,
Tyler Michael J.,
Eichinger Peter C. H.
Publication year - 2008
Publication title -
rapid communications in mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.528
H-Index - 136
eISSN - 1097-0231
pISSN - 0951-4198
DOI - 10.1002/rcm.3723
Subject(s) - tree frog , chemistry , edman degradation , complementary dna , peptide , peptide sequence , antimicrobial peptides , frog skin , microbiology and biotechnology , biochemistry , gene , biology , zoology , organic chemistry , sodium
The glandular skin secretion of the Eastern Dwarf Tree Frog Litoria fallax contains nine peptides named fallaxidins. The sequences of these peptides were elucidated using a combination of positive and negative electrospray mass spectrometry together with Edman sequencing. Among these peptides are: (i) fallaxidins 1.1 and 2.1 which have the sequences YFPIPI‐NH 2 and FWPFM‐NH 2 . The activities of these peptides are unknown, but it has been shown that they are not smooth muscle active, opioids or antimicrobially active, nor do they effect proliferation of lymphocytes; (ii) two weakly active antibiotics, fallaxidins 3.1 and 3.2 (e.g. fallaxidin 3.1, GLLDLAKHVIGIASKL‐NH 2 ), and a moderately active antibiotic fallaxidin 4.1 (GLLSFLPKVIGVIGHLIHPPS‐OH). Fallaxidin 4.1 has an unusual sequence for an antibiotic, containing three Pro residues together with a C‐terminal CO 2 H group. cDNA cloning has confirmed the identity of the nine isolated peptides from L . fallax , together with five additional peptides not detected in the peptide profile. The pre‐regions of the nine preprofallaxidins are conserved and similar to those of the caerin peptides from L . caerulea and L . splendida , suggesting that the fallaxidin and caerin peptides, although significantly different in sequence, originated from a common ancestor gene. Copyright © 2008 John Wiley & Sons, Ltd.