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The engineered pept...
The engineered peptide construct NCAM1-Aβ inhibits fibrillization of the human prion protein (PrP)
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Gielnik, Maciej (författare)
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Zhukova, Lilia (författare)
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Zhukov, Igor (författare)
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- Gräslund, Astrid (författare)
- Stockholms universitet,Institutionen för biokemi och biofysik
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Kozak, Maciej (författare)
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- Wärmländer, Sebastian K. T. S. (författare)
- Stockholms universitet,Institutionen för biokemi och biofysik
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(creator_code:org_t)
- 2022-02-10
- 2022
- Engelska.
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Ingår i: Acta Biochimica Polonica. - : Polskie Towarzystwo Biochemiczne (Polish Biochemical Society). - 0001-527X .- 1734-154X. ; 69:1, s. 257-261
- Relaterad länk:
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https://doi.org/10.1...
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https://ojs.ptbioch....
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- 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.
Ämnesord
- NATURVETENSKAP -- Biologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences (hsv//eng)
Nyckelord
- Creutzfeldt-Jakob disease
- AFM imaging
- amyloid
- drug design
- drug transport
- protein-peptide interaction
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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