Open AccessThe engineered peptide construct NCAM1-Aβ inhibits fibrillization of the human prion protein (PrP)
Author(s) -
Maciej Gielnik,
Lilia Zhukova,
Igor Zhukov,
Astrid Gräslund,
Maciej Kozak,
Sebastian K.T.S. Wärmländer
Publication year - 2022
Publication title -
acta biochimica polonica
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.452
H-Index - 78
eISSN - 1734-154X
pISSN - 0001-527X
DOI - 10.18388/abp.2020_5679
Subject(s) - peptide , chemistry , prion protein , infectivity , amyloid (mycology) , cell penetrating peptide , biophysics , cell , amyloid fibril , fibril , protein aggregation , microbiology and biotechnology , amyloid β , biochemistry , virology , biology , disease , virus , medicine , inorganic chemistry , pathology
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.