Journal
BIOMACROMOLECULES
Volume 14, Issue 1, Pages 27-37Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bm301165u
Keywords
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Funding
- University College Dublin
- Irish Research Council for Science, Engineering and Technology (IRCSET)
- European Union [COST TD0802, FOOD-CT-2004-506579]
- Irish Department of Agriculture, Food, and Rural Development [FIRM 01-RD-D160]
- Czech National Cost Project [OC10053]
- Swiss project POLYDEN
- SER
- Saxon Ministry for Science and Art
- German Ministry for Education and Science
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Prion diseases are characterized by the accumulation of PrPSc, an aberrantly folded isoform of the host protein PrPC. Specific forms of synthetic molecules known as dendrimers are able to eliminate protease resistant PrPSc in both an intracellular and in vitro setting The properties of a dendrimer which govern this ability are unknown. We addressed the issue by comparing the in vitro antiprion ability of numerous modified poly(propylene-imine) dendrimers, which varied in size, structure, charge, and surface group composition. Several of the modified dendrimers, including an anionic glycodendrimer, reduced the level of protease resistant PrPSc in a prion strain-dependent manner. This led to the formulation of a new working model for dendrimer/prion interactions which proposes dendrimers eliminate PrPSc by destabilizing the protein and rendering it susceptible to proteolysis. This ability is not dependent on any particular charge of dendrimer, but does require a high density of reactive surface groups.
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