Nanobodies raised against monomeric ɑ-synuclein inhibit fibril formation and destabilize toxic oligomeric species

D Klenerman, M Iljina, L Hong, Mathew Horrocks, MH Ludtmann, ML Choi, Craig Hughes, Francesco Ruggeri, T Guilliams, AK Buell, Jieun Lee, S Gandhi, Steven Lee, Clare Bryant, Michele Vendruscolo, Tuomas Knowles, Christopher Dobson, E De Genst & David Klenerman
$\textbf{Background:}$ The aggregation of the protein ɑ-synuclein (ɑS) underlies a range of increasingly common neurodegenerative disorders including Parkinson’s disease. One widely explored therapeutic strategy for these conditions is the use of antibodies to target aggregated ɑS, although a detailed molecular-level mechanism of the action of such species remains elusive. Here, we characterize ɑS aggregation in vitro in the presence of two ɑS-specific single-domain antibodies (nanobodies), NbSyn2 and NbSyn87, which bind to the highly accessible C-terminal...
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