Sunday, November 30

NASA Joins the Search for the Alzheimer's Cure

SpaceX Falcon 9 Rocket
Alzheimer's begins when "tau" fibers get tangled. Preventing this tangling may hold the cure to Alzheimer's. But how? Researchers cannot study this process in the lab because Earth's gravity causes tau fibers to settle before they can tangle. Now, NASA has stepped up with the answer. Learn about America's space launch of "Self-Assembly in Biology and the Origin of Life (SABOL): A Study into Alzheimer's."



Florida Institute of Technology researchers won a prestigious grant enabling them to launch a groundbreaking experiment on a flight to the International Space Station (ISS). Their proposal, "Self-Assembly in Biology and the Origin of Life (SABOL): A Study into Alzheimer's," was just one of seven "labs-in-a-box" chosen to make the spectacular trip in the International Space Station Research Competition.

Space: The Final Alzheimer's Frontier

The experiment recently launched into space on a trip to the International Space Station via a SpaceX Falcon 9 rocket from Cape Canaveral Air Force Station.

The principal investigators on this research are former astronaut Sam Durrance, Florida Tech professor of physics and space sciences, and College of Engineering faculty members Daniel Kirk and Hector Gutierrez. The work is based on earlier discoveries by Shaohua Xu.

"Through our project we seek to develop an improved understanding of the origin of life on our planet, increase our understanding of Alzheimer's disease and provide an opportunity to apply this new understanding for the betterment of humanity," said Durrance.

Why Space?

Durrance leads the biological science experiment, which will investigate the spontaneous assembly of amyloid proteins into long linear fibers. In Alzheimer's, accumulation of linear amyloid fibers composed of either tau proteins or amyloid-β peptides have been shown to self-organize in solution through colloidal interactions.

However, the mechanisms of amyloid fiber assembly are difficult to study on Earth because the protein fibers settle, which prevents further growth. In weightlessness they should stay suspended and continue growing with multiple fibers wrapping around each other into helical fiber bundles. The analysis of these fiber bundles should provide a clearer understanding of the internal structure of the amyloid fibers.

"It isn't clear whether amyloid deposits are the cause or a symptom of the disease, or whether they will form in vivo (in a living organism) the same way they form in vitro (in a test tube), but it is clear that a complete understanding of the colloidal formation process will greatly benefit neurodegenerative disease research," said Durrance. The researchers believe that understanding the colloidal chemistry and biochemistry of amyloid fiber formation should lead to strategies for controlling the process.

What Will Happen Up There?

The experiment will include about nine different incubation periods from one day to 30 days during orbit operations. When the buffer solution and protein powder are mixed and the temperature is set, it takes about a day to agglomerate into protein spheres, a few days to form fibers and a week or more to become tangling fibers, which in 30 days on Earth, would settle.

Kirk and Gutierrez are co-directors of Florida Tech's Aerospace Systems and Propulsion (ASAP) Laboratory.

The experiment, which will be contained in a payload box unit called a NanoLab Module — a four-inch cube—can be manipulated and monitored from Florida Tech laboratories while it is in flight. "One of our challenges is to make everything very small and automated," said Durrance.

How It Came About

Dr. Shaohua Xu began developing this theory in 1997, when he conducted Mad Cow disease research at the University of Chicago. In 2008, using the new technology of atomic force microscopy, Xu observed for the first time the actual process by which Alzheimer's fibers develop. Since then, he has been able to synthesize the fibers from purified tau protein. He says, "It's a three-step process:
  1. First, molecules of the tau protein cluster together into spheres, each almost the same size.
  2. Next, the spheres join in linear chains like beads on a string.
  3. In the third stage, the beads merge together to form a uniform filament identical to those found in the brains of Alzheimer's patients."
Xu says, "The process we have observed closely resembles that of colloid formation. Colloids are mixtures like milk or ink in which tiny particles are suspended in a fluid. Our theory is based on colloid science."

Xu affirms that if he is on the right track, it may be possible to halt the disease with drugs that hinder the aggregation of the spherical colloidal particles into linear chains. Similar chemicals are already used to stabilize artificial colloidal materials such as inks and paints.

How Big is the Potential Breakthrough?

Advocates of Xu's theory include KSC physician Daniel Woodard, the first medical doctor to review the research. He says, "Shaohua's theory is revolutionary; his evidence is overwhelming. The medical implications are beyond anything in my experience."

NASA physician David Tipton, chief of the Aerospace Medicine and Environmental Health Branch at KSC, says, "This could be the most important biomedical discovery ever made at Kennedy Space Center."

Additionally, Pamela Tronetti, medical director of the Parrish Senior Consultative Center, predicts, "If this theory is correct, it may well have as great an impact on neurodegenerative disease as the discovery of germs had on infection."

MORE INFORMATION:

About Florida Institute of Technology
Founded at the dawn of the Space Race in 1958, Florida Tech is the only independent, technological university in the Southeast. The university is designated a Tier One Best National University in U.S. News & World Report, and is one of just nine schools in Florida lauded by the 2012 Fiske Guide to Colleges and recognized by Bloomberg Businessweek as the best college for return on investment in Florida. Additional information is available online at www.fit.edu
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