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The amyloid-inhibit...
The amyloid-inhibiting NCAM-PrP peptide targets Aβ peptide aggregation in membrane-mimetic environments
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- Król, Sylwia (author)
- Stockholms universitet,Institutionen för biokemi och biofysik
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- Österlund, Nicklas (author)
- Stockholms universitet,Institutionen för biokemi och biofysik
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- Vosough, Faraz (author)
- Stockholms universitet,Institutionen för biokemi och biofysik
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- Jarvet, Jüri (author)
- Stockholms universitet,Institutionen för biokemi och biofysik
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- Wärmländer, Sebastian (author)
- Stockholms universitet,Institutionen för biokemi och biofysik
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- Barth, Andreas (author)
- Stockholms universitet,Institutionen för biokemi och biofysik
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- Ilag, Leopold Luna (author)
- Stockholms universitet,Institutionen för material- och miljökemi (MMK)
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Magzoub, Mazin (author)
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- Gräslund, Astrid (author)
- Stockholms universitet,Institutionen för biokemi och biofysik
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- Mörman, Cecilia (author)
- Stockholms universitet,Institutionen för biokemi och biofysik
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(creator_code:org_t)
- Elsevier BV, 2021
- 2021
- English.
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In: iScience. - : Elsevier BV. - 2589-0042. ; 24:8
- Related links:
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https://doi.org/10.1...
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http://www.cell.com/...
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https://urn.kb.se/re...
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Abstract
Subject headings
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- Substantial research efforts have gone into elucidating the role of protein misfolding and self-assembly in the onset and progression of Alzheimer’s disease (AD). Aggregation of the Amyloid-β (Aβ) peptide into insoluble fibrils is closely associated with AD. Here, we use biophysical techniques to study a peptide-based approach to target Aβ amyloid aggregation. A peptide construct, NCAM-PrP, consists of a largely hydrophobic signal sequence linked to a positively charged hexapeptide. The NCAM-PrP peptide inhibits Aβ amyloid formation by forming aggregates which are unavailable for further amyloid aggregation. In a membrane-mimetic environment, Aβ and NCAM-PrP form specific heterooligomeric complexes, which are of lower aggregation states compared to Aβ homooligomers. The Aβ:NCAM-PrP interaction appears to take place on different aggregation states depending on the absence or presence of a membrane-mimicking environment. These insights can be useful for the development of potential future therapeutic strategies targeting Aβ at several aggregation states.
Subject headings
- NATURVETENSKAP -- Kemi (hsv//swe)
- NATURAL SCIENCES -- Chemical Sciences (hsv//eng)
Publication and Content Type
- ref (subject category)
- art (subject category)
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- By the author/editor
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Król, Sylwia
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Österlund, Nickl ...
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Vosough, Faraz
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Jarvet, Jüri
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Wärmländer, Seba ...
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Barth, Andreas
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show more...
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Ilag, Leopold Lu ...
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Magzoub, Mazin
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Gräslund, Astrid
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Mörman, Cecilia
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- About the subject
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- NATURAL SCIENCES
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NATURAL SCIENCES
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and Chemical Science ...
- Articles in the publication
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iScience
- By the university
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Stockholm University