Author:
Gielnik Maciej,Zhukova Lilia,Zhukov Igor,Gräslund Astrid,Kozak Maciej,Wärmländer Sebastian K.T.S.
Abstract
AbstractIn prion diseases, the prion protein (PrP) becomes misfolded and forms fibrillar aggregates, which are resistant to proteinase degradation and become responsible for prion infectivity and pathology. So far, no drug or treatment procedures have been approved for prion disease treatment. We have previously shown that engineered cell-penetrating peptide constructs can reduce the amount of prion aggregates in infected cells. The molecular mechanisms underlying this effect are however unknown. Here, we use atomic force microscopy (AFM) imaging to show that the aggregation of the human PrP protein can be inhibited by equimolar amounts of the 25 residues long engineered peptide construct NCAM1-Aβ.
Publisher
Cold Spring Harbor Laboratory
Cited by
2 articles.
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