Beet compound may help slow progression of Alzheimer's disease: Study

A compound in beet plant that gives the vegetable its distinctive red colour may help slow the progression of Alzheimer's disease, a study claims.

Researchers at the University of South Florida in the US found that the compound could slow the accumulation of misfolded proteins in the brain, a process associated with Alzheimer's.

The discovery could lead to the development of drugs that may alleviate some of the long-term effects of the disease, the world's leading cause of dementia, researchers said.

"Our data suggest that betanin, a compound in beet extract, shows some promise as an inhibitor of certain chemical reactions in the brain that are involved in the progression of Alzheimer's disease," said Li-June Ming from University of South Florida.

"This is just a first step, but we hope that our findings will encourage other scientists to look for structures similar to betanin that could be used to synthesise drugs that could make life a bit easier for those who suffer from this disease," said Ming, who presented the research at the national meeting of the American Chemical Society (ACS).

Scientists are still trying to figure out what causes this progressive and irreversible brain disorder.

However, one prime suspect is beta-amyloid, a sticky protein fragment, or peptide, that accumulates in the brain, disrupting communication between brain cells called neurons.

Much of this damage occurs, Ming said, when beta-amyloid attaches itself to metals such as iron or copper.

These metals can cause beta-amyloid peptides to misfold and bind together in clumps that can promote inflammation and oxidation - a process similar to rusting - in nearby neurons, eventually killing them.

Previous research conducted by other scientists suggests that beetroot juice can improve oxygen flow to the ageing brain and possibly improve cognitive performance.

Ming and colleagues wanted to find out if betanin, a beet compound used in commercial dyes that readily binds to metals, could block the effects of copper on beta-amyloid and, in turn, prevent the misfolding of these peptides and the oxidation of neurons.

They conducted a series of experiments involving 3,5 di-tert-butylcatechol, or DTBC.

The scientists measured the oxidative reaction of DTBC when exposed to beta-amyloid only, beta-amyloid bound to copper, and copper-bound beta-amyloid in a mixture containing betanin.

On its own, beta-amyloid caused little or no oxidation of DTBC, researchers said.

However, as expected, beta-amyloid bound to copper induced substantial DTBC oxidation.

When betanin was added to the copper-bound beta-amyloid mixture, the researchers found oxidation dropped by as much as 90 per cent, suggesting that misfolding of the peptides was potentially suppressed.