The engineered peptide construct NCAM1-Aβ inhibits fibrillization of the human prion protein (PrP).

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.

• Publication year

  2022

• Venue

  Acta Biochimica Polonica

• Publication date

  2022-02-10

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.18388/abp.2020_5679PMID 35143147
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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