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The Maculatin peptides from the skin glands of the tree frog Litoria genimaculata : a comparison of the structures and antibacterial activities of Maculatin 1.1 and Caerin 1.1
Author(s) -
Rozek Tomas,
Waugh Russell J.,
Steinborner Simon T.,
Bowie John H.,
Tyler Michael J.,
Wallace John C.
Publication year - 1998
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/(sici)1099-1387(199804)4:2<111::aid-psc134>3.0.co;2-8
Subject(s) - edman degradation , peptide , antibiotics , dorsum , antibacterial peptide , amino acid , fast atom bombardment , antibacterial activity , chemistry , peptide sequence , antimicrobial peptides , biochemistry , biology , mass spectrometry , bacteria , anatomy , chromatography , genetics , gene
Six peptides have been isolated and characterized from the dorsal glands of the tree frog Litoria genimaculata . One of these is the known hypotensive peptide caerulein; the others have been named maculatins. The amino acid sequences of the maculatin peptides have been determined using a combination of fast atom bombardment mass spectrometry and automated Edman sequencing. Four of the maculatin peptides show antibiotic activity, with maculatin 1.1 [GLFGVLAKVAAHVVPAIAEHF(NH 2 ;)] showing the most pronounced activity, particularly against Gram‐positive organisms. Maculatin 1.1 resembles the known caerin 1 antibiotic peptides, except that four of the central amino acid residues (of the caerin 1 system) are missing in maculatin 1.1. A comparison of the antibiotic activity of maculatin 1.1 with those of caerin 1.1 is reported. ©1998 European Peptide Society and John Wiley & Sons, Ltd.