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Influence of Surface Groups on Poly(propylene imine) Dendrimers Antiprion Activity
Date Issued
2012-12-12
Date Available
2013-04-15T13:35:18Z
Abstract
Prion diseases are characterized by the accumulation of PrP(Sc), an aberrantly folded isoform of the host protein PrP(C). Specific forms of synthetic molecules known as dendrimers are able to eliminate protease-resistant PrP(Sc) 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 PrP(Sc) in a prion strain-dependent manner. This led to the formulation of a new working model for dendrimer/prion interactions which proposes dendrimers eliminate PrP(Sc) 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.
Type of Material
Journal Article
Publisher
American Chemical Society
Journal
Biomacromolecules
Volume
14
Issue
1
Start Page
27
End Page
37
Copyright (Published Version)
2012, American Chemical Society
Keywords
Language
English
Status of Item
Peer reviewed
This item is made available under a Creative Commons License
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