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RESEARCH

 

Inspired by Surfaces and Biomolecules

We aim to understand complex biological processes taking place at surfaces and interfaces using novel spectroscopic techniques with a high-surface sensitivity. The interface between two media may act as a driving force for many biological processes to proceed. For instance, it has been shown that at the surface of water, proteins can show a different conformation. Such a conformationally-altered protein might have a strong tendency to aggregate and to form insoluble fiber-like aggregates. 

 
 
Schematics showing the proposed mechanism of the amyloid-β (Aβ) peptide fibril formation.

Schematics showing the proposed mechanism of the amyloid-β (Aβ) peptide fibril formation.

A MULTI-SPECTROSCOPIC APPROACH TO PROBE AMYLOID AGGREGATION AT BIOLOGICAL SURFACES

The 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 the growth and development of 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. Although substantial knowledge on the aggregation process of proteins in the bulk solution exists, the influence of the cell membrane on this process is poorly understood. Most recent research emphasizes the importance of membrane for amyloid fibril formation in vivo. It was suggested that composition, charge, and hydrophobicity of the lipid membrane and especially raft domains, enriched in cholesterol and sphingolipids, may strongly enhance fibrillogenesis. 

The aim of our study is to answer one of the most important questions in biology and chemistry:
what is the role of protein-membrane interaction in protein aggregation process?

To fully understand the mechanism of Aβ peptide interaction with lipid membranes, a technique which would allow determining protein secondary structure and meanwhile would be surface specific is needed. We will 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 a 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. The aim of our study is to answer one of the most important questions in biology and chemistry: what is the role of protein-membrane interaction in protein aggregation process?

The importance of the described research project has been recognized by the European Commission and Dr. Simona Strazdaite was granted a Marie Skłodowska-Curie fellowship to work on this project. The project started on the 1st of June 2018 and will continue to last for 24 months. During the first year of the proposed research, a model system – lysozyme will be used for the initial study of fibrils formation. Lysozyme is very suitable as a model system because it is well studied with various techniques and has a relatively simple structure. After the completion of experiments on the model system, during the second year of the proposed research, we will study amyloid-β (Aβ) peptide, which is associated with Alzheimer’s syndrome. 

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The progress of this project
will be regularly updated on this website, so stay tuned!