Peptides From Australian Frogs. The Structures of the Dynastins From the Banjo Frogs Limnodynastes interioris, Limnodynastes dumerilii and Limnodynastes terraereginae

Abstract

The dermal glandular extracts of the tibial (calf) glands of the Australian banjo frogs Limnodynastes interioris, Limnodynastes dumerilii and Limnodynastes terraereginae each contain a different peptide, which we have named dynastin 1, 2 and 3 respectively. The determination of the sequences of these peptides is detailed.

Antimicrobial peptides from amphibian skin: What do they tell us?

“…85,86 FIGURE 6 cDNA-derived amino acid sequences of the preproregion from the precursors of frog skin peptides. Identical residues are boldfaced.…”

The Negative Ion Mass Spectra of [M-H]− Ions Derived From Caeridin and Dynastin Peptides. Internal Backbone Cleavages Directed Through Asp and Asn Residues

“…The caeridin peptide 6 co-occurs with succinimide derivative 7 in the skin of Litoria gilleni. 5 The internal succinimide is formally formed by cyclization between the CO 2 H of the Asp side chain and the amide nitrogen of the adjacent Gly. The spectrum of the [M-H] -ion of 7 is shown in Fig.…”

“…The B and (Y + 2) backbone cleavages 8 of the MH + ions often provide the full amino acid sequence of the caeridin and dynastin peptides; in other cases at least 80% of the sequence can be so determined. [1][2][3][4][5] During the last decade, we have studied the fragmentations of the [M-H] -ions of small underivatized peptides (for reviews see Ref. 9).…”

“…[1][2][3][4][5] Amongst the latter are the caeridins (from Litoria species [1][2][3] ) and the dynastins (from Limnodynastes species 4,5 ), whose molecular weights range from 850 to 1600 Da. In our structural studies [1][2][3][4][5] of these peptides, we used a combination of fast-atom bombardment (FAB) mass spectrometry, Edman degradation mass spectrometry, 6 and automated Edman sequencing 7 to determine the amino acid sequences. The B and (Y + 2) backbone cleavages 8 of the MH + ions often provide the full amino acid sequence of the caeridin and dynastin peptides; in other cases at least 80% of the sequence can be so determined.…”

An Overview of Brevinin Superfamily: Structure, Function and Clinical Perspectives

“…Magainins exhibit broad-spectrum antimicrobial activity, inhibiting the growth of both Gram positive and Gram negative bacteria, Candida albicans, Cryptococcus neoformansand, Saccharomyces cerevisiae and also demonstrated to induce lysis in several protozoan species (Zasloff 1987). Those discoveries stimulated great interest in amphibian skin peptides (Bevins and Zasloff 1990;Rafferty et al 1993). These peptides are stored in granular glands, which are localized mostly in the skin of dorsal area and are surrounded by myocytes and innervated by sympathetic fibers (Simmaco et al 1998;Simmaco et al 1994).…”