Low levels of toxic proteins linked to brain diseases, study suggests

Neurodegenerative diseases such as Alzheimer's could be better understood thanks to insight into proteins linked to such conditions, a study suggests.

Scientists studying thread-like chains of protein – called amyloid fibres – have found that low levels of these proteins may cause more harm to health than high levels.

These rarely formed protein chains, which have been linked with dozens of diseases, are produced as a result of a or changes in body chemistry brought about by ageing.

When this happens, short fibres are formed which become sticky and attract copies of themselves, forming an endless chain. These chains spontaneously break, creating more filament ends to which more proteins attach.

In the context of neurodegenerative diseases, it is these short, broken pieces that seem to be most harmful, scientists say.

Researchers have found that when are low, lots of short protein threads are formed. But when protein levels are high, this spontaneous breakage stops and most remain long.

Compared with harmful short protein fibres, long fibres do not appear to be damaging in the case of . Researchers therefore believe that high levels of the protein – which lead to these longer chains – may actually be protective.

In addition to shedding light on disease, this insight into the protein chains may help scientists develop useful biomaterials, such as cell scaffolds, which are used for tissue engineering or to make artificial silk.

Cait MacPhee, Professor of Biological Physics at the University of Edinburgh's School of Physics and Astronomy, said; "We would expect that the higher the level of toxins, the worse the disease. However, in this study we found that the lower the level of the protein, the more of these damaging short fibres we see. Understanding how these protein chains form offers us insight not only into how diseases progress, but how we can produce controlled for tissue engineering."

More information: The study is published in Nature Communications.

add to favorites email to friend print save as pdf

Related Stories

Order from disorder

May 02, 2012

NPL and University of Leicester scientists have explored a new way of ordering proteins for materials engineering at the nanoscale, using natural biological phenomena as a guide.

Hybrid material as gold-leaf substitute

Jun 18, 2013

(Phys.org) —A team of researchers headed by Professor Raffaele Mezzenga has created a hybrid material out of gold and milk proteins that looks like a wafer-thin gold leaf. Thanks to its properties, it could ...

Recommended for you

Student seeks to improve pneumonia vaccines

5 hours ago

Almost a million Americans fall ill with pneumonia each year. Nearly half of these cases require hospitalization, and 5-7 percent are fatal. Current vaccines provide protection against some strains of the ...

Seabed solution for cold sores

6 hours ago

The blue blood of abalone, a seabed delicacy could be used to combat common cold sores and related herpes virus following breakthrough research at the University of Sydney.

Better living through mitochondrial derived vesicles

Aug 19, 2014

(Medical Xpress)—As principal transformers of bacteria, organelles, synapses, and cells, vesicles might be said to be the stuff of life. One need look no further than the rapid rise to prominence of The ...

Zebrafish help to unravel Alzheimer's disease

Aug 19, 2014

New fundamental knowledge about the regulation of stem cells in the nerve tissue of zebrafish embryos results in surprising insights into neurodegenerative disease processes in the human brain. A new study by scientists at ...

Engineering new bone growth

Aug 19, 2014

MIT chemical engineers have devised a new implantable tissue scaffold coated with bone growth factors that are released slowly over a few weeks. When applied to bone injuries or defects, this coated scaffold ...

User comments