Natural Protein Implicated in Alzheimer’s Disease May Benefit Human Health

by Shirley Johanna on  August 1, 2015 at 3:25 PM Research News   - G J E 4
A protein involved in the progression of Alzheimer's disease also has properties that could benefit human health, says a new research.
Natural Protein Implicated in Alzheimer’s Disease May Benefit Human Health
Natural Protein Implicated in Alzheimer’s Disease May Benefit Human Health

A shorter form of a protein called beta amyloid is present both in diseased and healthy brains, said the study that could help researchers better understand how Alzheimer's develops.

"We know that the shorter form of beta amyloid is present in the diseased brain, but we now know that it is abundant in healthy brains as well," said lead researcher Simon Drew from University of Melbourne in Australia.

Shorter version of this protein may act as a sponge that safely binds a metal that can damage brain tissue when it is in excess, the findings showed.

In the late 1990s, high levels of copper were discovered within the clumps of beta amyloid formed in people with Alzheimer's disease. Copper is essential to health, but too much can produce harmful free radicals.

Many scientists began to suspect that this copper might be contributing to the disease. They found that beta-amyloid can bind to copper indiscriminately and allow it to produce these damaging free radicals.

Closer analysis of beta amyloid protein has revealed different sizes.

"The small change in length makes a huge difference to its copper binding properties. We found that the short form of the protein is capable of binding copper at least 1000 times stronger than the longer forms. It also wraps around the metal in a way that prevents it from producing free radicals," Drew explained.

"Given these properties and its relative abundance, we can speculate this type of beta amyloid is protective. It is very different from the current view of how beta amyloid interacts with biological copper," Drew noted in a statement released by University of Melbourne.

Source: IANS

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