Neuroscience

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Posts tagged amyloid protein

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Alzheimer-substance may be the nanomaterial of tomorrow 
It causes brain diseases like Alzheimer’s, Parkinson’s and Creutzfeldt-Jakob’s disease. It is also hard and rigid as steel. Now research at Chalmers University of Technology shows that the amyloid protein carries unique characteristics that may lead to the development of new composite materials for nano processors and data storage of tomorrow and even make objects invisible.
Piotr Hanczyc, PhD student at the department of Chemical and Biological Engineering, shows in an article in Nature Photonics, that the amyloid, a very dense aggregate of protein that causes brain diseases like Alzheimer’s and Parkinson’s, carries unique characteristics. Unlike well-functioning protein the amyloid reacts upon multi photon laser irradiation. This laser may in the future possibly be used for detection of amyloids inside a human brain. This discovery is in itself a breakthrough.
- But you can also create these aggregates in an artificial way in a laboratory and in combination with other materials create unique characteristics, Piotr Hanczyc says.
The amyloid aggregates are as hard and rigid as steel. The difference is that steel is much heavier and has defined material properties whereas amyloids can be tuned for desired purpose. By attaching a material’s molecules to the dense amyloid its characteristics change. This has been known for more than ten years and is already used by scientists.
- What hasn’t been known is that the amyloids react to multi-photon irradiation and this opens up new possibilities to also change the nature of the material attached to the amyloids, Piotr Hanczyc says.
The amyloids are shaped like discs densely piled upon each other.  When a material gets merged with these discs its molecules end up so densely and regularly that they can communicate and exchange information. This means totally new possibilities to change a material’s characteristics.
Multi-photon tests on materials tied to amyloids are yet to be performed, but Piotr sees an opportunity for cooperation with Chalmers material science researchers interested for example in solar cell technology.
And though it may still be science fiction, he also considers that one day scientists may use the material properties of amyloid fibrils in the research of invisible metamaterials.
- An object’s ability to reflect light could be altered so that what’s behind it gets reflected instead of the object itself, in principle changing the index of light refraction, kind of like when light hits the surface of water, Piotr Hanczyc says.

Alzheimer-substance may be the nanomaterial of tomorrow

It causes brain diseases like Alzheimer’s, Parkinson’s and Creutzfeldt-Jakob’s disease. It is also hard and rigid as steel. Now research at Chalmers University of Technology shows that the amyloid protein carries unique characteristics that may lead to the development of new composite materials for nano processors and data storage of tomorrow and even make objects invisible.

Piotr Hanczyc, PhD student at the department of Chemical and Biological Engineering, shows in an article in Nature Photonics, that the amyloid, a very dense aggregate of protein that causes brain diseases like Alzheimer’s and Parkinson’s, carries unique characteristics. Unlike well-functioning protein the amyloid reacts upon multi photon laser irradiation. This laser may in the future possibly be used for detection of amyloids inside a human brain. This discovery is in itself a breakthrough.

- But you can also create these aggregates in an artificial way in a laboratory and in combination with other materials create unique characteristics, Piotr Hanczyc says.

The amyloid aggregates are as hard and rigid as steel. The difference is that steel is much heavier and has defined material properties whereas amyloids can be tuned for desired purpose. By attaching a material’s molecules to the dense amyloid its characteristics change. This has been known for more than ten years and is already used by scientists.

- What hasn’t been known is that the amyloids react to multi-photon irradiation and this opens up new possibilities to also change the nature of the material attached to the amyloids, Piotr Hanczyc says.

The amyloids are shaped like discs densely piled upon each other.  When a material gets merged with these discs its molecules end up so densely and regularly that they can communicate and exchange information. This means totally new possibilities to change a material’s characteristics.

Multi-photon tests on materials tied to amyloids are yet to be performed, but Piotr sees an opportunity for cooperation with Chalmers material science researchers interested for example in solar cell technology.

And though it may still be science fiction, he also considers that one day scientists may use the material properties of amyloid fibrils in the research of invisible metamaterials.

- An object’s ability to reflect light could be altered so that what’s behind it gets reflected instead of the object itself, in principle changing the index of light refraction, kind of like when light hits the surface of water, Piotr Hanczyc says.

Filed under amyloid protein alzheimer's disease amyloid fibres neurodegenerative diseases science

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Lasers might be the cure for brain diseases such as Alzheimer’s and Parkinson’s
Researchers at Chalmers University of Technology in Sweden, together with researchers at the Polish Wroclaw University of Technology, have made a discovery that may lead to the curing of diseases such as Alzheimer’s, Parkinson’s and Creutzfeldt-Jakob disease (the so called mad cow disease) through photo therapy.
The researchers discovery, which was published yesterday in the journal Nature Photonics, is that it is possible to distinguish aggregations of the proteins, believed to cause the diseases, from the the well-functioning proteins in the body by using multi-photon laser technique.
“Nobody has talked about using only light to treat these diseases until now. This is a totally new approach and we believe that this might become a breakthrough in the research of diseases such as Alzheimer’s, Parkinson’s and Creutzfeldt-Jakob disease. We have found a totally new way of discovering these structures using just laser light”, says Piotr Hanczyc at Chalmers University of Technology.
If the protein aggregates are removed, the disease is in principle cured. The problem until now has been to detect and remove the aggregates.
The researchers now harbor high hopes that photo acoustic therapy, which is already used for tomography, may be used to remove the malfunctioning proteins. Today amyloid protein aggregates are treated with chemicals, both for detection as well as removal. These chemicals are highly toxic and harmful for those treated.
With multi photon laser the chemical treatment would be unnecessary. Nor would surgery be necessary for removing of aggregates. Due to this discovery it might, thus, be possible to remove the harmful protein without touching the surrounding tissue.
These diseases arise when amyloid beta protein are aggregated in large doses so they start to inhibit proper cellular processes.
Different proteins create different kinds of amyloids, but they generally have the same structure. This makes them different from the well-functioning proteins in the body, which can now be shown by multi photon laser technique.

Lasers might be the cure for brain diseases such as Alzheimer’s and Parkinson’s

Researchers at Chalmers University of Technology in Sweden, together with researchers at the Polish Wroclaw University of Technology, have made a discovery that may lead to the curing of diseases such as Alzheimer’s, Parkinson’s and Creutzfeldt-Jakob disease (the so called mad cow disease) through photo therapy.

The researchers discovery, which was published yesterday in the journal Nature Photonics, is that it is possible to distinguish aggregations of the proteins, believed to cause the diseases, from the the well-functioning proteins in the body by using multi-photon laser technique.

“Nobody has talked about using only light to treat these diseases until now. This is a totally new approach and we believe that this might become a breakthrough in the research of diseases such as Alzheimer’s, Parkinson’s and Creutzfeldt-Jakob disease. We have found a totally new way of discovering these structures using just laser light”, says Piotr Hanczyc at Chalmers University of Technology.

If the protein aggregates are removed, the disease is in principle cured. The problem until now has been to detect and remove the aggregates.

The researchers now harbor high hopes that photo acoustic therapy, which is already used for tomography, may be used to remove the malfunctioning proteins. Today amyloid protein aggregates are treated with chemicals, both for detection as well as removal. These chemicals are highly toxic and harmful for those treated.

With multi photon laser the chemical treatment would be unnecessary. Nor would surgery be necessary for removing of aggregates. Due to this discovery it might, thus, be possible to remove the harmful protein without touching the surrounding tissue.

These diseases arise when amyloid beta protein are aggregated in large doses so they start to inhibit proper cellular processes.

Different proteins create different kinds of amyloids, but they generally have the same structure. This makes them different from the well-functioning proteins in the body, which can now be shown by multi photon laser technique.

Filed under alzheimer's disease parkinson's disease Creutzfeldt-Jakob disease multi-photon laser amyloid protein science

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New chemical approach to beat Alzheimer’s disease
Scientists at the University of Liverpool and Callaghan Innovation in New Zealand have developed a new chemical approach to help harness the natural ability of complex sugars to treat Alzheimer’s disease.
The team used a new chemical method to produce a library of sugars, called heparan sulphates, which are known to control the formation of the proteins in the brain that cause memory loss.
Chemically produced in the lab
Heparan sulphates are found in nearly every cell of the body, and are similar to the natural blood-thinning drug, heparin. Now scientists have discovered how to produce them chemically in the lab, and found that some of these sugars can inhibit an enzyme that creates small proteins in the brain.
These proteins, called amyloid, disrupt the normal function of cells leading to the progressive memory loss that is characteristic of Alzheimer’s disease.
Professor Jerry Turnbull, from the University’s Institute of Integrative Biology, said: “We are targeting an enzyme, called BACE, which is responsible for creating the amyloid protein. The amyloid builds up in the brain in Alzheimer’s disease and causes damage. BACE has proved to be a difficult enzyme to block despite lots of efforts by drug companies.”
“We are using a new approach, harnessing the natural ability of sugars, based on the blood-thinning drug heparin, to block the action of BACE.”
Dr Peter Tyler, from Callaghan Innovation, added: “We have developed new chemical methods that have allowed us to make the largest set of these sugars produced to date. These new compounds will now be tested to identify those with the best activity and fewest possible side effects, as these have potential for development into a drug treatment that targets the underlying cause of this disease.”
Current treatments only help symptoms
There are more than 800,000 people in the UK, and 50,000 in New Zealand living with dementia. Over half of these have Alzheimer’s disease, the most common cause of dementia. The cost of these diseases to the UK economy stands at £23 billion, more than the cost of cancer and heart disease combined. Current treatments for dementia can help with symptoms, but there are no drugs available that can slow or stop the underlying disease.

New chemical approach to beat Alzheimer’s disease

Scientists at the University of Liverpool and Callaghan Innovation in New Zealand have developed a new chemical approach to help harness the natural ability of complex sugars to treat Alzheimer’s disease.

The team used a new chemical method to produce a library of sugars, called heparan sulphates, which are known to control the formation of the proteins in the brain that cause memory loss.

Chemically produced in the lab

Heparan sulphates are found in nearly every cell of the body, and are similar to the natural blood-thinning drug, heparin. Now scientists have discovered how to produce them chemically in the lab, and found that some of these sugars can inhibit an enzyme that creates small proteins in the brain.

These proteins, called amyloid, disrupt the normal function of cells leading to the progressive memory loss that is characteristic of Alzheimer’s disease.

Professor Jerry Turnbull, from the University’s Institute of Integrative Biology, said: “We are targeting an enzyme, called BACE, which is responsible for creating the amyloid protein. The amyloid builds up in the brain in Alzheimer’s disease and causes damage. BACE has proved to be a difficult enzyme to block despite lots of efforts by drug companies.”

“We are using a new approach, harnessing the natural ability of sugars, based on the blood-thinning drug heparin, to block the action of BACE.”

Dr Peter Tyler, from Callaghan Innovation, added: “We have developed new chemical methods that have allowed us to make the largest set of these sugars produced to date. These new compounds will now be tested to identify those with the best activity and fewest possible side effects, as these have potential for development into a drug treatment that targets the underlying cause of this disease.”

Current treatments only help symptoms

There are more than 800,000 people in the UK, and 50,000 in New Zealand living with dementia. Over half of these have Alzheimer’s disease, the most common cause of dementia. The cost of these diseases to the UK economy stands at £23 billion, more than the cost of cancer and heart disease combined. Current treatments for dementia can help with symptoms, but there are no drugs available that can slow or stop the underlying disease.

Filed under alzheimer’s disease memory loss heparan sulphates amyloid protein neuroscience science

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