David J. M. Stone

Peptides from Australian frogs. Structures of the caerins and caeridin 1 from Litoria splendida

Seven peptides have been isolated from the parotoid and rostral glands of the Australian green tree frog Litoria splendida. These include caerulein (a known hypotensive toxin), and six new compounds named caerin 1.1 (M, 2582), 1.1.1 (2412), 1.1.2 (2299), 2.1 (2392), 3.1 (2382) and caeridin 1 (1139). The primary structures of the peptides have been determined by FAB mass spectrometric methods, and confirmed by automated sequencing. The major peptides have been synthesised using t-BOC (N-tert-butoxycarbonyl)N-protection and a p-methylbenzhydrylamine support.

The structure of caerin 1.1, a novel antibiotic peptide from Australian tree frogs

The structure of caerin 1.1, a novel peptide with biological activity from Australian tree frogs, is determined on the basis of mass spectrometric data; the peptides primary sequence prevents it from achieving a complete α-helix.

The Edman degradation of vancomycin: preparation of vancomycin hexapeptide

The preparation and characterisation of the hexapeptides derived from vancomycin and vancomycin CDP-1 by Edman degradation are described.

Peptides from Australian frogs. Structures of the caeridins from Litoria caerulea

The secretions of the parotoid glands of the Australian tree frog Litoria caerulea contain twenty-five peptides of which six, the caeridins, have molecular weights in the 1100–1550 dalton range. The paper describes the primary structures of the caeridins, and indicates how the exudates caeridin composition varies with the geographic location of the species.