A protein that makes it possible for whales to dive for up to two hours without breathing could pave way for the development of synthetic blood that could potentially save lives, findings of a new study suggest.
Researchers have been searching for ways to develop synthetic blood for use in human trauma patients. Many hospitals depend on donated whole blood but these tend to be in short supply and have limited storage life.
Now, John Olson, from Rice University, and colleagues found that whales have a more stable version of myoglobin, a protein crucial for storing oxygen inside muscle cells, which could possibly be harnessed to create synthetic blood.
For the new study, first published online in the Journal of Biological Chemistry on July 23, Olson, who has spent two decades studying hemoglobin with the aim of creating synthetic blood that can be used in transfusions, and his team discovered that that the deep-diving mammals have very stable versions of myoglobin that do not have the tendency to unfold.
Such stability can be attributed as to why the whale's cells produce large amounts of the protein and which explains why whales have muscle cells that are far more loaded with myoglobin compared to those in humans.
By having up to 20 times more myoglobin in their muscles, whales can stay active regardless if they hold their breath for long periods of time at great depths.
Olson wanted to create a strain of genetically-engineered bacteria that can generate a molecule based on myoglobin, which happens to be similar albeit simpler in structure than hemoglobin, the protein that allows blood to transport oxygen as well as make some corpuscles in the blood red.
The researchers said that whale myoglobin can be produced up to several times the quantity of humans for the same effort and while their works have not yet developed a synthetic blood, they said that they have developed methods that will allow them to identify more stable recombinant hemoglobin that can one day be used to substitute blood.
"This work is very important for our projects on synthetic blood substitutes and determining the toxicity of acellular hemoglobin," Olson said. "Premila has laid the groundwork for high-throughput screening of large libraries of hemoglobin variants without the need for purifying milligram quantities of pure protein. This method is a big step forward in our efforts to identify more stable recombinant hemoglobins."
