cone snail faster insulin

NEWS

NEWS

REPORT

Insulin derived from cone snail venom

could make insulin action much faster.

SNAILSULIN

A

n international team

of researchers have

developed the smallest,

fully functional version of

insulin, combining human

insulin with the fast-acting potential of a

venom insulin produced by predatory

cone snails.

Cone snails, found slithering across

coral reefs, are constantly on the prowl for

prey. Some, such as Conus geographus,

release plumes of toxic venom that

contain a unique form of insulin into the

surrounding water. This causes fish blood

glucose levels to plummet, temporarily

paralysing them so the snail can take its

prey.

In earlier studies, the researchers

discovered that this venomous insulin had

many biochemical traits in common with

human insulin - and it appears to work

faster than the quickest-acting human

insulin currently available.

Faster-acting insulin would diminish

the risk of hyperglycaemia and other

serious complications of diabetes, says

Helena Safavi, Ph.D., a study co-author

and an assistant professor of biomedical

sciences at the University of Copenhagen

in Denmark. It also could improve the

performance of insulin pumps or artificial

pancreas devices, which automatically

release insulin into the body as needed.

Slightly unhinged

The researchers found that insulin derived

from cone snail venom lacks a 'hinge'

component that causes human insulin to

aggregate or clump together so it can be

stored in the pancreas. These aggregates

must break up into individual molecules

before they can begin to work on blood

sugar, a process that can take up to an

hour. Since cone snail insulin doesn't

aggregate, it is, in essence, primed and

ready to work on the body's biochemical

machinery almost immediately.

Intrigued, the researchers began to

investigate ways to transform the insulin

that cone snails use as a weapon into a

different form: one that people who have

Type-1 diabetes could use to rapidly

restore equilibrium in their bodies.

"We had the idea of making human

insulin more snail-like," says Safavi, "so,

we sought to basically take some of

the advantageous properties from the

snail and graft them onto the human

compound."

The researchers thought this was

possible because cone snail insulin

essentially has the same basic structure

or 'backbone' as human insulin. However,

the snail's insulin is far less potent than

human insulin, and the researchers

suspect that humans would require 20 to

30 times more of the cone snail insulin to

lower their blood sugar levels.

In this new study, Dr Danny HungChieh

Chou, Ph.D, one of the study's

corresponding authors, sought to

overcome these problems. First, they

used structural biology and medicinal

chemistry techniques to isolate four

amino acids that help the snail insulin bind

to the insulin receptor. Then, they created

a truncated version of a human insulin

molecule without the region responsible

for clumping.

The team integrated modified versions

of these amino acids into the human

molecule in hopes of creating a hybrid

that does not clump and binds the human

insulin receptor with high potency.

Mini revolution

In tests with laboratory rats, this hybrid

insulin molecule, which the scientists

call "mini-insulin," interacted with insulin

receptors in ways that cone snail insulin

doesn't. These new interactions bound

mini-insulin to insulin receptors in the rat's

body just as strongly as normal human

insulin would. As a result, mini-insulin had

the same potency as human insulin but

acted faster.

"Mini-insulin has tremendous

potential," Chou says. "With just a

few strategic substitutions, we have

generated a potent, fast-acting molecular

structure that is the smallest, fully active

insulin to date. Because it is so small, it

should be easy to synthesise, making it

a prime candidate for the development of

a new generation of insulin therapeutics."

"We now have the capability to create

a hybrid version of insulin that works in

humans, and that also appears to have

many of the positive attributes of cone

snail insulin," says Chou. "That's an

important step forward in our quest to

make diabetes treatment safer and more

effective."

The study appears in Nature Structural

and Molecular Biology.

a potent, fast-acting

molecular structure

that is the smallest,

fully active insulin

to date - Dr Danny

Hung-Chieh Chou

"

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