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FEBS Lett. 2008 Feb 20;582(4):517-22. doi: 10.1016/j.febslet.2008.01.014. Epub 2008 Jan 28.

Anti-oligomeric single chain variable domain antibody differentially affects huntingtin and alpha-synuclein aggregates.

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Department of Chemical Engineering, Arizona State University, Tempe, AZ 85287, USA.


Huntington's and Parkinson's diseases are both neurodegenerative disorders caused at least in part by misfolding and aggregation of huntingtin (htt) and alpha-synuclein, respectively. Here we use a single chain antibody fragment (scFv) isolated against oligomeric alpha-synuclein to probe similarities and differences between the aggregation and toxic mechanisms of htt and alpha-synuclein. When incubated with htt, the scFv both blocks formation of and promotes dissociation of fibrillar aggregates, but stabilizes formation of cytotoxic oligomeric aggregates. Previous studies with monomeric alpha-synuclein showed the scFv prevented fibrillar aggregation, but blocked toxicity of oligomeric aggregates. These divergent effects suggest the toxic mechanisms of oligomeric aggregates differ among amyloidogenic protein species.

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