The engineered peptide construct NCAM1-Aβ inhibits fibrillization of the human prion protein (PrP)
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Published:2022-02-10
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ISSN:1734-154X
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Container-title:Acta Biochimica Polonica
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language:
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Short-container-title:Acta Biochim Pol
Author:
Gielnik Maciej,Zhukova Lilia,Zhukov Igor,Gräslund Astrid,Kozak Maciej,Wärmländer Sebastian
Abstract
In prion diseases, the prion protein (PrP) becomes misfolded and forms fibrillar aggregates that are 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. However, the molecular mechanism underlying this effect is unknown. Here, we use atomic force microscopy (AFM) imaging to show that the amyloid aggregation and fibrillization of the human PrP protein can be inhibited by equimolar amounts of the 25 residues long engineered peptide construct NCAM1-Aβ.
Publisher
Polskie Towarzystwo Biochemiczne (Polish Biochemical Society)
Subject
General Biochemistry, Genetics and Molecular Biology
Cited by
2 articles.
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