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New pharmacological tools from a haematophagus (Vampire) snail, Colubraria reticulata, have been discovered. these include anaesthetic peptides, haemostasis inhibitors and vasoconstriction modulators see paper. The authors note that fish appear to be semi anaethetised when the snail is in close proximity and this enables the snail to extend it's probosis and collect the fishes blood.

With the domination of classical antibiotics coming to a dramatic end, it is time to find novel sources of antibiotics that circumvent the ability of the bacterial to evolve resistance.

New classes of antibiotics are being found in the venoms of several species. Screening these as you would for other compounds is already yielding promising results.

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Once more the theraphosids (Tarantulas) have delivered novel tools for targeting pain relevant ion channels. A novel NaV1.7 blocking peptide has been identified from the species Grammostolla porteri (pictured). This peptide has 1000x fold selectivity over NaV1.5 and 20x over NaV1.4. However mutational analysis and structural analysis has allowed for modification to increase the NaV1.4 selectivity to 1000x also. Thus producing an excellent tool for pain research and potential novel therapeutic. Abstract here

Sicarius terrosus (six-eyed cave spider) is a highly toxic (and somewhat infamous) spider of the sicariidae family, whose bites, however rare, are characterised by significant necrotic pathology and potential mortality.  This is largely because of the presence of sphingomyelinase D in its venom[1], in the form of Phospholipase D StSicTox-betaIC1[2].  This has been shown to cause dermonecrosis in mammals[3] as well as being a potent insecticide[4].  Additionally an StSicTox-beta IF1 variant is present, which similarly catalyses sphingomyelin hydrolysis[5], does so with low effectiveness and does not cause dermonecrosis, blood vessel permeability and platelet aggregation.  Two cytochrome C oxidase subunits[6][7] (catalyses reduction of O₂ to H₂O) are found in this venom, as well as reserves of NADH dehydrogenase[8].

[1] http://www.ncbi.nlm.nih.gov/pubmed/23991242

[2] http://www.uniprot.org/uniprot/C1ITQ4

[3] http://www.ncbi.nlm.nih.gov/pubmed/19042943

[4] http://www.ncbi.nlm.nih.gov/pubmed/22561243

[5] http://www.uniprot.org/uniprot/C0JB54

[6] http://www.uniprot.org/uniprot/C1ITQ4

[7] http://www.uniprot.org/uniprot/C1ITQ3

[8] http://www.uniprot.org/uniprot/B8R334