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The Structures of the Frenatin Peptides from the Skin Secretion of the Giant Tree Frog Litoria Infrafrenata
Author(s) -
Raftery M. J.,
Waugh R. J.,
Bowie J. H.,
Wallace J. C.,
Tyler M. J.
Publication year - 1996
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.60
Subject(s) - tree frog , frog skin , dorsum , peptide , amino acid , chemistry , secretion , amino acid residue , biology , neuropeptide , anatomy , peptide sequence , biochemistry , zoology , receptor , organic chemistry , gene , sodium
The granular dorsal glands of the giant tree frog Litoria infrafrenata contain five peptides including caerulein (a known neuropeptide), and four new peptides named frenatins 1 (MH + = 1140 Da), 2 (1423), 3 (2180) and 4 (2493). The amino acid sequences of the frenatins are detailed: their structures do not correspond to those of peptides isolated from other amphibians or animals. Frenatin 3, Gly‐Leu‐Met‐Ser‐Val‐Leu‐Gly‐His‐Ala‐Val‐Gly‐Asn‐Val‐Leu‐Gly‐ Gly‐Leu‐Phe‐Lys‐Pro‐Lys‐Ser‐(OH), has wide spectrum antimicrobial properties.