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Researcher from Wrocław on the trail of harmful proteins

14.08.2017 Health, Recommended

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We still know little about the properties or the formation process of amyloids - incorrectly formed protein molecules, which accumulate in the body and are associated with Alzheimer's disease, among other things. These molecules are being investigated by Dr. Joanna Olesiak-Bańska from Wroclaw University of Technology.

The primary goal of the project conducted by Dr. Joanna Olesiak-Bańska from the Faculty of Chemistry, Wroclaw University of Technology, is investigating the properties of amyloids - incorrectly formed protein molecules that accumulate in the body. Amyloids are associated with neurodegenerative diseases such as Alzheimer's disease and Parkinson's disease. It is easy to imagine that in the longer term these results could be used in the work on improving the diagnostics of these diseases.

 

"At present, diagnostics of amyloid-related diseases is primarily based on an interview, an evaluation of the person's behaviour" - Dr. Olesiak-Bańska told PAP. "It's possible to do a magnetic resonance scan, but amyloid deposits - harmful proteins accumulating in various organs - are only visible when they are very large, which means not much can be done about them. The technique that we propose potentially can detect smaller deposits and warn in advance that higher amyloid levels indicate a disease".

 

Hope for a thorough understanding of the properties of amyloids, according to the researcher from Wrocław, is in the study of their potential liquid crystal properties.

 

"Liquid crystals are materials that behave like a liquid, but their molecules are well ordered" - the researcher explained. "This means that they are on the border between liquid and crystal. Because the molecules are ordered, they have optical properties and can be easily imaged".

 

Why exactly could this be important? "We do not know exactly how amyloids are formed" - admited Dr. Olesiak-Bańska. "At first we only have one incorrectly formed protein molecule. Later, in an unknown way, it attaches to other molecules, thus building amyloids. If we could confirm that amyloid deposits are liquid crystals, we could start to investigate and describe the formation of such deposits using the techniques and mechanisms that we currently use to study liquid crystals" - she said.

 

"The main goal of our project is to develop a new amyloid imaging method. We are going to combine two methods that together can lead to this" - the researcher noted.

 

What does that mean? Researchers from Wrocław intend to use multi-photon microscopy to investigate the nonlinear optical properties of amyloids. They will try to strengthen these effects using nanoparticles of gold.

 

"Each material has optical properties that describe how it absorbs and emits light" - explained Dr. Olesiak-Bańska. "Nonlinear optical properties determine how efficiently the material (in this case, amyloid) absorbs light when it is subject to multiphoton excitation. But it is important that the material is not illuminated by a conventional light or low power laser - instead, it is excited with a high power pulse laser, which results in multiphoton processes" - she noted.

 

Researchers believe that nonlinear effects can be strengthened by gold nanoparticles - which would allow to improve the amyloid imaging process.

 

"The sizes of gold nanoparticles used in our project range from 10 to about 100 nanometers" - said Dr. Olesiak-Bańska. "Gold in this form has completely new optic properties: it allows us to modify the laser light that illuminates a sample of material. This allows, for example, to very strongly strengthen this light locally, as well as induce photothermal effects with it - convert radiation into heat energy".

 

"All this happens in the vicinity of the nanoparticle - which means that even when illuminating a large area of the material we can very accurately modify only the areas directly in contact with the particle" - the researcher said.

 

The project "NONA - nonlinear optics, nanoparticles and amyloids" was co-financed by the Foundation for Polish Science with the amount of PLN 1.7 million in the third competition of the FIRST TEAM programme.

 

PAP - Science and Scholarship in Poland, Katarzyna Florencka

 

kflo/ zan/ kap/

 

tr. RL

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