Amyloids are a type of protein that forms fibril-like aggregates. Their secondary structure is rich in β-sheet motifs. These represent a target binding site for fluorescent molecular probes, which can be attached to magnetic nanoparticles via biotin–streptavidin interaction and used in research on early detection of certain neurodegenerative diseases. This bachelor’s thesis presents the binding of a fluorescent molecular probe to biotin via a diethylene glycol linker, which was achieved through a multiple-step approach. First, a linker was synthesized using tert-butyl (2-(2-(2-hydroxyethoxy)ethoxy)ethyl)carbamate and succinic anhydride. A fluorescent molecular probe, (E)-2-(methyl(4-(2-nitrovinyl)phenyl)amino)ethan-1-ol, prepared from
4-((2-hydroxyethyl)(methyl)amino)benzaldehyde by the Henry reaction, was then coupled to it via Steglich esterification. This yielded an N-Boc protected compound to which biotin, activated by PyBOP reagent, was bound after the removal of a Boc protecting group.
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