Insulin in sea snail venom could be used by drug developers

By Dan Stanton

- Last updated on GMT

Cone snails could be a source of pharma ingredients
Cone snails could be a source of pharma ingredients
Venom produced by sea snails could be used in designing human insulin analogues or as painkiller drugs, according to a University of Utah scientist.

Cone snails are venomous by their nature, but an upcoming study in the Proceedings of the National Academy of Sciences (PNAS) journal finds insulin produced by some species is mixed in with venom toxins to send fish into hypoglycemic shock.

Lead author Helena Safavi-Hemami, a research assistant professor at the University of Utah, told in-Pharmatechnologist.com the insulin shares its basic structure with human insulin and some of the amino acids are identical, and could – like with other components of cone snails – be of interest to pharmaceutical developers.

“The likelihood that this insulin will ever be used to treat diabetes is very slim and we won’t pursue this avenue,”​ she said. “However, we believe that by comparing the activity and speed of action of this insulin compared to human insulin it may become a useful tool for better drug design of human insulin analogues.”

The research is still in its infancy, and bringing the ingredient into a preclinical setting is “still quite far away,” Safavi-Hemami added. “First we need to find out whether the venom insulin is active in human cells and whether it acts rapidly.”

The insulin is unique in it is shorter than any insulin that has been described in any animal. “We believe that it may act faster because it’s small and because of its streamlined role in rapid prey capture.”

Whether pharma R&D teams will be able to use these findings, already several compounds from cone snails have been investigated for their use as analgesics, including one compound which has received US FDA and EMA approval, as the gallery below shows.

The challenges in synthetically producing insulin taken from cone snails are due to the disulfide bonds that connect the two parts of the insulin molecule.

“The venom insulin we found has the same number of disulfide bonds and is therefore not easier to synthesize,”​ Safavi-Hemami told us. “However, we developed a technique to easier connect these bonds and would like to explore this technique further in the future.”

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