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|Title:||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|
|Citation:||Journal of Peptide Science, 1998; 4(2):111-115|
|Publisher:||JOHN WILEY & SONS LTD|
|Tomas Rozek, Russell J. Waugh, Simon T. Steinborner, John H. Bowie, Michael J. Tyler, John C. Wallace|
|Abstract:||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(NH2)] 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.|
|Keywords:||Litoria genimaculata; skin glands; glandular secretions; peptides; antibiotic activity; maculatins 1; caerin 1.1|
|Rights:||© 1998 European Peptide Society and John Wiley & Sons, Ltd.|
|Appears in Collections:||Biochemistry publications|
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