New discovery by German scientists that small heat shock proteins can prevent uncontrolled clumping of
proteins in the brain has opened a new frontier in developing drugs for Alzheimer’s
treatment. The accumulation of beta amyloid plaques (abnormal clusters of
chemically sticky protein fragments) between nerve cells in the brain is one of
the hallmarks of Alzheimer’s disease.
Alzheimer’s disease is the most common form of dementia. It
is fatal and progressive. The accumulation of amyloid plaques and
neurofibrillary tangles are the prime suspects behind damage and death of nerve
cells that destroy a person’s memory and cognitive skills.
There is no cure for Azlheimer’s but different drug and
non-drug therapies can make a person live ably with the disease. [Read more 15 Reasons Why You Should Eat More Fish]
Alzheimer’s is the 6th leading cause of death in
the United States. An estimated 5.1 million Americans have Alzheimer’s.
In the UK, an estimated 850,000 people will have dementia by
the end of 2015 and the number will rise to 1 million by 2025. Every year
nearly 60,000 deaths are directly attributed to dementia.
Small heat shock
proteins act as “helper” proteins and for the cells, they are the “catastrophe
aid workers”. They play a wide range of roles, including guarding other
proteins from becoming damaged. When vital cell proteins are exposed to intense
heat or radiation, they lose their form and clot up, turning into entangled
clumps. When the clumps are formed, these cells cannot be saved – they become
useless and begin to die. That’s when the small heat shock proteins come to the
rescue.
They bind to the damaged proteins before they clod together helping
them to restore their proper shape by preserving them in a soluble form. [Read more Scientists report significant breakthrough in anti-aging]
In Alzheimer’s disease, the small heat shock protein that
stops the beta-amyloid from forming long fibrils and clog up cells in the brain
is called alpha-B-crystallin.
The research team led by Bernd Reif, a chemistry professor
at the Technical University of Munich (TUM) and a team from Helmholtz Zentrum
München, shows exactly how alpha-B-crystallin collaborates with beta-amyloid to
stop the formation of clumping in Alzheimer’s.
The researchers were able to identify the exact locations in
the alpha-B-crystallin that bind to the beta-amyloid by using solid-state
Nuclear Resonance (NMR) spectroscopy. [এসপারাগাসঃ স্বাস্থ্যগুণ, ভেষজগুণ এবং ইতিহাস]
"Alpha-B-crystallin exists in various different forms
comprising 24, 28 or 32 subunits that are permanently being swapped. In
addition, it has a large molecular weight. These factors make structure
analysis very difficult,” Professor Reif explained the complexity of
alpha-B-crystallin.
Prof. Reif and his colleagues – Johannes Buchner, and
Sevil Weinkauf, both from TUM, found that these small heat shock protein
utilizes a certain non-polar beta-sheet form mound in its center for
communications with the beta-amyloid. This mechanism enables it to gain access to
the aggregation process in 2 locations at once –
1.
It attaches to dissolved beta-amyoids, stopping
them from formation of fibrils.
2.
It seals existing fibrils, therefore no more amyloids
cannot accumulate.
For further study, the researchers want to closely examine
the alpha-B-crystallin’s N-terminal region. As they discovered, it attaches to
protein types that clump together in a disorderly fashion.
The research was published in the journal Nature Structural & Molecular Biology.
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