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Translocation of the food-related amyloid fibrils hen egg-white lysozyme and α-Synuclein in in vitro cell models of the epithelial intestinal barrier For the evaluation of risks associated with amyloid fibrils

Doorn, M.S. (2021) Translocation of the food-related amyloid fibrils hen egg-white lysozyme and α-Synuclein in in vitro cell models of the epithelial intestinal barrier For the evaluation of risks associated with amyloid fibrils.

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Abstract:Amyloid fibrils are associated risks for the development of neurodegenerative diseases. Amyloid fibrils are not only naturally present in the human body, but are also found in food. Two amyloid fibril forming proteins found in food are the net positively charged hen egg-white lysozyme and α-Synuclein, which is net negatively charged. Hen egg-white lysozyme and α-Synuclein fibrils can cross-seed α-Synuclein, present in for example neurons, which can lead to aggregation into amyloid fibrils. This makes exposure to fibrils of the food-related proteins a potential risk for neurodegenerative diseases if these fibrils find their way to the brain. For this research, the α-Syn A53T variant of α-Synuclein is used to model animal α-Synuclein. The goal of this project was to examine the differences of lysozyme and α-Syn A53T fibrils in permeability characteristics across in vitro cell models to evaluate the risk of amyloid fibril exposure. As a first step towards developing a methodology to quantify the permeability of the in vitro cell models of the epithelial intestinal barrier, polystyrene nanobeads were used. The results of this research indicate that hen egg-white lysozyme, can cross the in vitro intestinal epithelial cell models used in this study more easily than α-Syn A53T, which is used as a model for animal α-Syn. This difference may be due to the charge difference, which can lead to different internalization properties. The exact nature of the permeated amyloid fibrils and the internalization mechanism should be further analyzed.
Item Type:Essay (Master)
Faculty:TNW: Science and Technology
Subject:33 physics, 42 biology, 50 technical science in general
Programme:Biomedical Engineering MSc (66226)
Link to this item:http://purl.utwente.nl/essays/86392
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