AM UNUSUAL COMBINATION OF PEPTIDES FROM THE SKIN GLANDS OF EWINGS TREE FROG, LITORIA-EWINGI - SEQUENCE DETERMINATION AND ANTIMICROBIAL ACTIVITY

Citation
St. Steinborner et al., AM UNUSUAL COMBINATION OF PEPTIDES FROM THE SKIN GLANDS OF EWINGS TREE FROG, LITORIA-EWINGI - SEQUENCE DETERMINATION AND ANTIMICROBIAL ACTIVITY, Australian Journal of Chemistry, 50(9), 1997, pp. 889-894
Citations number
38
Categorie Soggetti
Chemistry
ISSN journal
00049425
Volume
50
Issue
9
Year of publication
1997
Pages
889 - 894
Database
ISI
SICI code
0004-9425(1997)50:9<889:AUCOPF>2.0.ZU;2-4
Abstract
The dorsal glandular skin extract of the brown tree frog Litoria ewing i contains six major peptides. The amino acid sequences of the peptide s were determined by using a combination of mass spectrometry and auto mated Edman sequencing. One of the peptides, caerin 1.1 [Gly Leu Leu S er Val Leu Gly Ser Val Ala Lys His Val Leu Pro His Val Val Pro Val Ile Ala Glu His Leu (NH2)], has been isolated previously from Australian tree frogs of the genus Litoria, and is a wide-spectrum antimicrobial agent. The roles of the other five peptides in the amphibian skin have not, as yet, been determined. The most abundant peptide, uperin 7.1 [ Gly Trp Phe Asp Val Val Lys His Ile Ala Ser Ala Val (NH2)], shows stru ctural similarity to the uperin group of antimicrobial peptides isolat ed from toadlets of the genus Uperoleia (except that uperin 7.1 lacks the final four amino acid residues of uperins from the genus Uperoleia ). The significance of this finding hinges upon the distant evolutiona ry relationship of Litoria and Uperoleia. If the structural similarity implies a single evolutionary origin, it also implies a conservation of structural origin for at least 100 million years. Evolutionary conv ergence is a more likely explanation for the structural similarity of the peptides from the two genera. A related peptide, uperin 7.1.1, lac ks the first two amino acid residues from the N-terminal end of uperin 7.1. Uperin 7.1 exhibits minor antimicrobial activity while uperin 7. 1.1. is inactive. The three other peptides are caeridin 7.1 [Gly Leu L eu Asp Met Val Thr Gly Leu Leu Gly Asn Leu (NH2)] and two modified pep tides of the tryptophyllin group which we have named tryptophyllin 6.1 [Leu Phe Phe Trp Gly(NH2)] and 7.1 [Ile Phe Phe Phe Pro (NH2)]. Trypt ophyllins 6.1 and 7.1 are related to similar peptides isolated from th e Australian red tree frog Litoria rubella: such peptides may be neuro transmitters or neuromodulators.