Molecule Stops Alzheimer’s in its Tracks

In the war against Alzheimer’s disease, one of the big villains is a protein called amyloid beta—”Abeta” for short.

In a diseased brain, sticky strands of the protein clump into plaques that kill nerve cells and choke the gaps between them. Under a microscope the plaques look sinister, even to the untrained eye—scattershot black blotches, splattered across healthy tissue.

Amyloid beta plaques (Credit: Nephron/Wikimedia Commons)

Scientists, knowing the damage Abeta can cause, have searched for therapies that clear the protein from the brains of Alzheimer’s patients. So far, all clinical trials of this approach have failed. Though two trials are still ongoing, for now Alzheimer’s remains a disease with no prevention, treatment, or cure.

Now Carmela Abraham, Boston University professor of biochemistry and medicine, and colleagues have discovered a new way to attack Abeta. Instead of clearing it from the brain, the scientists have found a compound that prevents the body from making it in the first place.

The work, funded by the Alzheimer’s Association and the Cure Alzheimer’s Fund, may eventually lead to a novel treatment for this deadly disease.

“Alzheimer’s is now the number six killer of adults in the United States. Deaths from breast cancer and heart disease keep dropping, but Alzheimer’s increases every year,” says Abraham. “Caring for Alzheimer’s patients costs over $200 billion per year. The estimate for 2050 is $1.1 trillion, which means it will completely break the health care system. We have to find a drug.”

The brain creates Abeta with enzymes that chop a larger protein, called the amyloid precursor protein (APP), into smaller bits. Sometimes, for reasons scientists don’t quite understand, two APP proteins join together in a process called dimerization, which ultimately leads to increased Abeta.

Abraham wondered: if scientists could stop dimerization, would that stop Abeta in its tracks? She decided to try.

Continue reading to learn the astonishing discovery she made.