Elucidation of structural Properties of amyloid-like Fibrils via Solid State NMR

Abstract: The invention of plastic has revolutionized people's life style not only by facilitating the storage and transportation of various goods but also by improving mechanical properties of mankind's technological advances. However, plastic is considered to be harmful, as it contains toxic chemical compounds which are accumulated due to its persistence. Therefore, plastic materials represent a threat to the wildlife, since its extensive use and disposal in landfills and natural habitats increased eminently. People's growing concern about the enviromental impact of pastic and its presence in the food chain led to reflections about designing biodegradable materials that potentially may replace a wide range of plastic materials. It has been found that materials made of specific proteins show plastic-like properties. These protein-based materials are both flexible and remarkable strong. Since proteins are available in great abundance and biodegradable, they are a promising source for creating such desired, environmental friendly materials. Although the physicochemical properties of protein-based material are well-established, the quality needs to be improved in order to make them viable for the market. For this purpose, the molecular structure which determines the physicochemical properties has to be analysed. Whey proteins for example form under non-physiological conditions highly ordered structures, called nanofibrils. These nanofibrils form fine-stranded networks which make the resulting material so flexible and remarkably strong. A well-established to determine the molecular structure of these nanofibrils is by means of Solid State Nuclear Magnetic Resonance (NMR) Spectroscopy. For example whey proteins are well known for forming nanofibrils due to their history of being associated with the development of degenerative diseases. For this reason, they may serve as excellent models for analyzing the molecular structure of amyloid fibrils. The aim of this research project is to determine the molecular structure of amyloid fibrils obtained from the whey protein β-lactoglobulin (β-lg). The major challenge hereby is to prepare isotopic laballed β-lg nanofibrils which is for Solid State NMR measurements required.