Explore the words cloud of the MultiSpecAMYLOID project. It provides you a very rough idea of what is the project "MultiSpecAMYLOID" about.
The following table provides information about the project.
VALSTYBINIS MOKSLINIU TYRIMU INSTITUTAS FIZINIU IR TECHNOLOGIJOS MOKSLU CENTRAS
|Coordinator Country||Lithuania [LT]|
|Total cost||130˙779 €|
|EC max contribution||130˙779 € (100%)|
1. H2020-EU.1.3.2. (Nurturing excellence by means of cross-border and cross-sector mobility)
|Duration (year-month-day)||from 2018-06-01 to 2020-05-31|
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|1||VALSTYBINIS MOKSLINIU TYRIMU INSTITUTAS FIZINIU IR TECHNOLOGIJOS MOKSLU CENTRAS||LT (VILNIUS)||coordinator||130˙779.00|
Treatment of neurodegenerative diseases, such as Alzheimer’s and Parkinson’s syndrome, is one of the biggest challenges of nowadays medicine. The success of the curing strongly depends on our understanding of chemical processes involved in developing these diseases. From a chemical point of view, these diseases are determined by uncontrolled neuropathological alterations such as aggregation of proteins and formation of insoluble fibrils, called amyloids. It is of paramount importance to fully understand the fibril formation on a molecular level in order to find ways how to inhibit the protein aggregation.
In the proposed research we focus on the aggregation of Aβ peptide, which is associated with Alzheimer’s disease. Although substantial knowledge on the aggregation process of Aβ peptide in the bulk solution exists, the influence of the cell membrane on this process is poorly understood due to the lack of surface specific techniques. Here we propose to study the aggregation of Aβ peptide at the surface of model lipid membranes with advanced surface specific spectroscopic methods: vibrational sum-frequency generation (VSFG) and shell-isolated nanoparticles-enhanced Raman spectroscopy (SHINERS). Such combined spectroscopic approach will enable to determine the molecular structure of the aggregates at every step of the fibril formation and to reveal the role of the membrane. Altogether the proposed research will give relevant insights by which membrane and various co-solutes promote the aggregation process.
The candidate, Dr. S. StrazdaitÄ— has returned to her home country after PhD studies in the Netherlands. She is currently employed as a senior research fellow in the Centre for Physical Sciences and Technology (FTMC) at Prof. Gediminas Niaura group. The researcher will bring a valuable experience of surface specific spectroscopy to FTMC and during the proposed project she will acquire new knowledge and will reach an independent scientific maturity.
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The information about "MULTISPECAMYLOID" are provided by the European Opendata Portal: CORDIS opendata.
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