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Type: Journal article
Title: Host defence peptides from the skin glands of the Australian Blue Mountains tree-frog Litoria citropa
Author: Wegener, K.
Wabnitz, P.
Carver, J.
Bowie, J.
Chia, B.
Wallace, J.
Tyler, M.
Citation: European Journal of Biochemistry, 1999; 265(2):627-637
Issue Date: 1999
ISSN: 0014-2956
Abstract: Nineteen citropin peptides are present in the secretion from the granular dorsal glands of the Blue Mountains tree-frog Litoria citropa; 15 of these peptides are also present in the secretion from the submental gland. Two major peptides, citropin 1.1 (GLFDVIKKVASVIGGL-NH2), citropin 1.2 (GLFDIIKKVASVVGGL-NH2) and a minor peptide, citropin 1.3 (GLFDIIKKVASVIGGL-NH2) are wide-spectrum antibacterial peptides. The amphibian has an endoprotease which deactivates these membrane-active peptides by removing residues from the N-terminal end: loss of three residues gives the most abundant degradation products. The solution structure of the basic peptide citropin 1.1 has been determined by NMR spectroscopy [in a solvent mixture of trifluoroethanol/water (1 : 1)] to be an amphipathic alpha-helix with well-defined hydrophobic and hydrophilic regions. The additional four peptides produced by the dorsal glands are structurally related to the antibacterial citropin 1 peptides but contain three more residues at their C-terminus [e.g. citropin 1.1.3 (GLFDVIKKVASVIGLASP-OH)]. These peptides show minimal antibacterial activity; their role in the amphibian skin is not known.
Keywords: Skin; Animals; Anura; Peptides; Antimicrobial Cationic Peptides; Proteins; Amphibian Proteins; Anti-Infective Agents; Circular Dichroism; Magnetic Resonance Spectroscopy; Sequence Analysis; Amino Acid Sequence; Models, Molecular; Molecular Sequence Data; Mass Spectrometry
RMID: 0030004050
DOI: 10.1046/j.1432-1327.1999.00750.x
Appears in Collections:Ecology, Evolution and Landscape Science publications

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