'Snow flea antifreeze protein' could help improve organ preservation

Jul 21, 2008
By creating an antifreeze protein found in the Canadian snow flea, scientists are reporting a development that could extend the storage life of donor organs. The figure shows representations of the unprecedented structure of the protein in its mirror image forms prepared by total chemical synthesis. Credit: Courtesy of Brad Pentelute

Scientists in Illinois and Pennsylvania are reporting development of a way to make the antifreeze protein that enables billions of Canadian snow fleas to survive frigid winter temperatures.

Their laboratory-produced first-of-a-kind proteins could have practical uses in extending the storage life of donor organs and tissues for human transplantation, the researchers indicate in a report scheduled for the July 9 issue of the Journal of the American Chemical Society.

In the study, Stephen B. H. Kent and colleagues point out that scientists have tried for years to decipher the molecular structure and produce from chemicals in a laboratory the so-called "snow flea antifreeze protein (sfAFP)." Those steps are critical for obtaining larger amounts of the protein, which exists naturally in only minute quantities in snow fleas. The larger synthetic quantities can be used for further research and potential medical and commercial uses, they say.

The researchers made synthetic sfAFP, and showed that it has the same activity as the natural protein. They also produced variants, including one form of sfAFP with a molecular architecture that is the reverse, or "mirror image," of natural sfAFP and different from any other protein found in living things on Earth. The mirror-image form of sfAFP appears less likely to trigger harmful antibodies and more resistant to destruction by natural enzymes, making it potentially more effective than the native form for use in organ and tissue preservation, the scientists note.

"Our most significant advance was the use of the two mirror image forms of the protein to determine the previously unknown crystal structure of this unique protein," said Kent. "That is a first in the history of protein X-ray crystallography."

Source: ACS

Explore further: Program predicts placement of chemical tags that control gene activity

add to favorites email to friend print save as pdf

Related Stories

Recommended for you

A refined approach to proteins at low resolution

Sep 19, 2014

Membrane proteins and large protein complexes are notoriously difficult to study with X-ray crystallography, not least because they are often very difficult, if not impossible, to crystallize, but also because ...

Base-pairing protects DNA from UV damage

Sep 19, 2014

Ludwig Maximilian University of Munich researchers have discovered a further function of the base-pairing that holds the two strands of the DNA double helix together: it plays a crucial role in protecting ...

Smartgels are thicker than water

Sep 19, 2014

Transforming substances from liquids into gels plays an important role across many industries, including cosmetics, medicine, and energy. But the transformation process, called gelation, where manufacturers ...

User comments : 0