University of Twente Student Theses

Login

Investigating 14-3-3’s Binding Site upon Interaction with α-Synuclein Through Microscale Thermophoresis Based Competitive Assay

Veldman, O.P. (2022) Investigating 14-3-3’s Binding Site upon Interaction with α-Synuclein Through Microscale Thermophoresis Based Competitive Assay.

[img] PDF
12MB
Abstract:Parkinson’s Disease (PD) is a neurodegenerative disease characterized by the aggregation of α-synuclein to form toxic multimers in the neuronal cells of the body and brain. It has been shown that the 14-3-3 protein family influences the aggregation of α-synuclein by binding its multimers, preventing misfolding and delaying aggregation. This insight forms opportunities for potential therapeutic approaches regarding the pathogenesis of PD. Here, we performed a competitive assay based on microscale thermophoresis and show that 14-3-3’s amphipatic binding pocket may potentially be involved in the interaction between α-synuclein multimers and 14-3-3 proteins.
Item Type:Essay (Bachelor)
Faculty:TNW: Science and Technology
Subject:42 biology, 50 technical science in general
Programme:Biomedical Technology BSc (56226)
Link to this item:https://purl.utwente.nl/essays/92114
Export this item as:BibTeX
EndNote
HTML Citation
Reference Manager

 

Repository Staff Only: item control page