Pseudocatalytic Antiaggregation Activity of Antibodies: Immunoglobulins Can Influence Α-Synuclein Aggregation at Substoichiometric Concentrations
Document Type
Article
Publication Date
2016
Keywords
Parkinson’s disease, Antibodies, Protein aggregation, α-Synuclein
Digital Object Identifier (DOI)
https://doi.org/10.1007/s12035-015-9148-8
Abstract
Protein aggregation is involved in a variety of diseases. Alteration of the aggregation pathway, either to produce less toxic structures or to increase aggregate clearance, is a promising therapeutic route. Both active and passive immunization has been used for this purpose. However, the mechanism of action of antibodies on protein aggregates is not completely clear especially given poor ability of antibodies to cross blood–brain barrier. Here, we have shown that antibodies can interfere with protein aggregation at substoichiometric concentrations (as low as 1:1000 antibody to protein ratio). This is an indication that antibodies interact with aggregation intermediates in chaperone-like manner altering the aggregation pathways at very low antibody levels. This observation supports earlier suggestions that antibodies can inhibit aggregation by interaction with low abundance aggregation intermediates.
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
Molecular Neurobiology, v. 53, p. 1949-1958
Scholar Commons Citation
Breydo, Leonid; Morgan, Dave; and Uversky, Vladimir N., "Pseudocatalytic Antiaggregation Activity of Antibodies: Immunoglobulins Can Influence Α-Synuclein Aggregation at Substoichiometric Concentrations" (2016). Molecular Medicine Faculty Publications. 343.
https://digitalcommons.usf.edu/mme_facpub/343
