umu.sePublications
Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Pro-Inflammatory S100A9 Protein Aggregation Promoted by NCAM1 Peptide Constructs
Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.ORCID iD: 0000-0002-1691-9025
Show others and affiliations
2019 (English)In: ACS Chemical Biology, ISSN 1554-8929, E-ISSN 1554-8937, Vol. 14, no 7, p. 1410-1417Article in journal (Refereed) Published
Abstract [en]

Amyloid cascade and neuroinflammation are hallmarks of neurodegenerative diseases, and pro-inflammatory S100A9 protein is central to both of them. Here, we have shown that NCAM1 peptide constructs carrying polycationic sequences derived from A beta peptide (KKLVFF) and PrP protein (KKRPKP) significantly promote the S100A9 amyloid self-assembly in a concentration-dependent manner by making transient interactions with individual S100A9 molecules, perturbing its native structure and acting as catalysts. Since the individual molecule misfolding is a rate-limiting step in S100A9 amyloid aggregation, the effects of the NCAM1 construct on the native S100A9 are so critical for its amyloid self-assembly. S100A9 rapid self assembly into large aggregated clumps may prevent its amyloid tissue propagation, and by modulating S100A9 aggregation as a part of the amyloid cascade, the whole process may be effectively tuned.

Place, publisher, year, edition, pages
AMER CHEMICAL SOC , 2019. Vol. 14, no 7, p. 1410-1417
National Category
Biophysics
Identifiers
URN: urn:nbn:se:umu:diva-162010DOI: 10.1021/acschembio.9b00394ISI: 000476957100005PubMedID: 31194501OAI: oai:DiVA.org:umu-162010DiVA, id: diva2:1342187
Available from: 2019-08-13 Created: 2019-08-13 Last updated: 2019-08-13Bibliographically approved

Open Access in DiVA

No full text in DiVA

Other links

Publisher's full textPubMed

Authority records BETA

Pansieri, JonathanOstojic, LucijaIashchishyn, IgorMorozova-Roche, Ludmilla

Search in DiVA

By author/editor
Pansieri, JonathanOstojic, LucijaIashchishyn, IgorSmirnovas, VytautasMorozova-Roche, Ludmilla
By organisation
Department of Medical Biochemistry and Biophysics
In the same journal
ACS Chemical Biology
Biophysics

Search outside of DiVA

GoogleGoogle Scholar

doi
pubmed
urn-nbn

Altmetric score

doi
pubmed
urn-nbn
Total: 60 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf