Novel Uperin Peptides From the Dorsal Glands of the Australian Floodplain Toadlet Uperoleia inundata

Bradford, AM; Raftery, MJ; Bowie, J.U.; Tyler, MJ; Jc, Wallace; Adams, GW; Severini, Cinzia

doi:10.1071/ch9960475

Cited by 17 publications

(12 citation statements)

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“…It is one of the most potent membrane-active antibiotic peptides isolated from amphibians and is particularly effective against Gram-positive organisms [8]. Citropin 1.1 is a 16 residue peptide and is one of a number of amphibian antibiotic peptides containing the characteristic Lys7-Lys8 pattern: a group which includes lesueurin (from L. lesueuri) [17], the aureins (from L. aurea and L. raniformis) [11] and the uperins (from toadlets of the genus Uperoleia) [68]. Citropin 1.1 does not cause lysis of red blood cells at a concentration of 100 lgAEmL )1 , but lysis is complete at 1 mgAEmL )1 (B. C. S. Chia & J. H. Bowie, unpublished results).…”

Section: Discussionmentioning

confidence: 99%

nNOS inhibition, antimicrobial and anticancer activity of the amphibian skin peptide, citropin 1.1 and synthetic modifications

Doyle

Brinkworth

Wegener

et al. 2003

European Journal of Biochemistry

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A large number of bioactive peptides have been isolated from amphibian skin secretions. These peptides have a variety of actions including antibiotic and anticancer activities and the inhibition of neuronal nitric oxide synthase. We have investigated the structure-activity relationship of citropin 1.1, a broad-spectrum antibiotic and anticancer agent that also causes inhibition of neuronal nitric oxide synthase, by making a number of synthetically modified analogues. Citropin 1.1 has been shown previously to form an amphipathic a-helix in aqueous trifluoroethanol. The results of the structure-activity studies indicate the terminal residues are important for bacterial activity and increasing the overall positive charge, while maintaining an amphipathic distribution of residues, increases activity against Gram-negative organisms. Anticancer activity generally mirrors antibiotic activity suggesting a common mechanism of action. The N-terminal residues are important for inhibition of neuronal nitric oxide synthase, as is an overall positive charge greater than three. The structure of one of the more active synthetic modifications (A4K14-citropin 1.1) was determined in aqueous trifluoroethanol, showing that this peptide also forms an amphipathic a-helix.

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Section: Discussionmentioning

confidence: 99%

nNOS inhibition, antimicrobial and anticancer activity of the amphibian skin peptide, citropin 1.1 and synthetic modifications

Doyle

Brinkworth

Wegener

et al. 2003

European Journal of Biochemistry

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“…Group II has only one member, Da-1039 (Fig. 6B), with only very limited homology to the uperin family of antibacterial frog skin secretions (Bradford et al, 1996;Steinborner et al, 1997). Group III comprise three 9e11 residue Dq toxins with moderate homology with the temporin family of antibacterial frog skin secretions (Abbassi et al, 2008;Rinaldi and Conlon, 2013;Simmaco et al, 1996).…”

Section: Dinoponeratoxinsmentioning

confidence: 99%

Diversity of peptide toxins from stinging ant venoms

Aili

Touchard

Escoubas³

et al. 2014

Toxicon

100

151

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Ants (Hymenoptera: Formicidae) represent a taxonomically diverse group of arthropods comprising nearly 13,000 extant species. Sixteen ant subfamilies have individuals that possess a stinger and use their venom for purposes such as a defence against predators, competitors and microbial pathogens, for predation, as well as for social communication. They exhibit a range of activities including antimicrobial, haemolytic, cytolytic, paralytic, insecticidal and pain-producing pharmacologies. While ant venoms are known to be rich in alkaloids and hydrocarbons, ant venoms rich in peptides are becoming more common, yet remain understudied. Recent advances in mass spectrometry techniques have begun to reveal the true complexity of ant venom peptide composition. In the few venoms explored thus far, most peptide toxins appear to occur as small polycationic linear toxins, with antibacterial properties and insecticidal activity. Unlike other venomous animals, a number of ant venoms also contain a range of homodimeric and heterodimeric peptides with one or two interchain disulfide bonds possessing pore-forming, allergenic and paralytic actions. However, ant venoms seem to have only a small number of monomeric disulfide-linked peptides. The present review details the structure and pharmacology of known ant venom peptide toxins and their potential as a source of novel bioinsecticides and therapeutic agents.

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“…5). A family of structurally related peptides, termed the uperins, has been isolated from the Australian frogs Uperoleia mjoberii [51] and Uperoleia inundata [52] that are active against Gram-positive bacteria. From the species Crinia signifera, two peptides differing by a single amino acid, termed signiferin 2.1 and signiferin 2.2, were identified that are also active against Gram-positive bacteria [53].…”

Section: Myobatrachidaementioning

confidence: 99%

Structural diversity and species distribution of host-defense peptides in frog skin secretions

Conlon

2011

Cell. Mol. Life Sci.

170

147

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Cationic peptides that adopt an amphipathic α-helical conformation in a membrane-mimetic environment are synthesized in the skins of many frog species. These peptides often display cytolytic activities against bacteria and fungi consistent with the idea that they play a role in the host's system of defense against pathogenic microorganisms, but their importance in the survival strategy of the animal is not clearly understood. Despite the common misconception that antimicrobial peptides are synthesized in the skins of all anurans, the species distribution is sporadic, suggesting that their production may confer some evolutionary advantage to the organism but is not necessary for survival. The low potency of many frog skin antimicrobial peptides is consistent with the hypothesis that cutaneous symbiotic bacteria may provide the major system of defense against pathogenic microorganisms in the environment with antimicrobial peptides assuming a supplementary role in some species.

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Novel Uperin Peptides From the Dorsal Glands of the Australian Floodplain Toadlet Uperoleia inundata

Cited by 17 publications

References 0 publications

nNOS inhibition, antimicrobial and anticancer activity of the amphibian skin peptide, citropin 1.1 and synthetic modifications

nNOS inhibition, antimicrobial and anticancer activity of the amphibian skin peptide, citropin 1.1 and synthetic modifications

Diversity of peptide toxins from stinging ant venoms

Structural diversity and species distribution of host-defense peptides in frog skin secretions

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