Venom of carnivorous sea snail could be fast-acting insulin for diabetics

Cone Snail — When the cone snail's venom is injected into fish, it elicits hypoglycemic shock or dangerously low blood glucose. YouTube

From alternative treatments to new discoveries, scientists are offering possible treatments for diabetes ignored before. One possible treatment is insulin from cone snail venom.

Sydney Morning Herald reports that biologists from the University of Utah discovered in 2015 specialised insulin used for chemical warfare by cone snails that hunt for fish. When the venom is injected into fish, it elicits hypoglycemic shock or dangerously low blood glucose, reports PNAS.

Researchers plan to make an artificial version of fast-acting insulin for use in humans. Eight amino acids composed human insulin, a protein which forms a hinge. Without the amino acids, the hinge mechanism would not work and insulin cannot bind to the receptor on the cells’ surface.

Regular insulin takes 15 minutes before it take effect among diabetic patients. Using the cone snail’s venom was a model, Mike Lawrence, structural biologist at the Walter and Eliza Hall Institute, says the effect of the next-generation insulins could be instantaneous for type 1, type 2 and gestational diabetics.

“Our breakthrough has been to determine the structure of this venom insulin,” Lawrence says. “The 'ah-ha moment' was realising that it doesn't have the hinge mechanism that human insulin does and then working out how it gets by without it,” he adds.

Lawrence explains that although the insulin was made by a sea snail, it was designed to work on fish which is a vertebrate species like humans. “Fish are closer to us than snails,” the biologist notes why he expects the snail venom’s insulin to be effective in humans.

Once the snail’s prey is into hypoglycaemic shock, its mollusk strikes and slurps it target. Because fish is fast-moving and the snail is not, a snail needs venom that is fast acting. The snail venom insulin has a smaller substitute for the hinge made up of just one amino acid.

The study, published in the Nature Structural and Molecular Biology on Tuesday, is an international collaboration which involved American and Danish researchers and scientists from Australian institutions, including the Walter and Eliza Hall Institute, Monash University, La Trobe University and Flinders University.

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