Nanobodies raised against monomeric α-synuclein inhibit fibril formation and destabilize toxic oligomeric species
Authors list
Marija Iljina Liu Hong Mathew H Horrocks Marthe H Ludtmann Minee Choi Craig D Hughes Francesco S Ruggeri Tim Guilliams Alexander K Buell Ji-Eun Lee Sonia Gandhi Steven F Lee Clare E Bryant Michele Vendruscolo Tuomas PJ Knowles Christopher M Dobson Erwin De Genst David KlenermanAbstract
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 region of ɑS.
Journal details
Journal BMC Biology
Volume 15
Issue number 1
Pages 57
Available online
Publication date
Full text links
Publisher website (DOI) 10.1186/s12915-017-0390-6
Europe PubMed Central 28673288
Pubmed 28673288
Keywords
Type of publication