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Pro-Inflammatory S100A9 Protein Aggregation Promoted by NCAM1 Peptide Constructs
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Rekke forfattare: 112019 (engelsk)Inngår i: ACS Chemical Biology, ISSN 1554-8929, E-ISSN 1554-8937, Vol. 14, nr 7, s. 1410-1417Artikkel i tidsskrift (Fagfellevurdert) 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.

sted, utgiver, år, opplag, sider
2019. Vol. 14, nr 7, s. 1410-1417
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Identifikatorer
URN: urn:nbn:se:su:diva-171791DOI: 10.1021/acschembio.9b00394ISI: 000476957100005PubMedID: 31194501OAI: oai:DiVA.org:su-171791DiVA, id: diva2:1346155
Tilgjengelig fra: 2019-08-27 Laget: 2019-08-27 Sist oppdatert: 2019-08-27bibliografisk kontrollert

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Wallin, CeciliaWärmländer, Sebastian K. T. S.Gräslund, AstridSmirnovas, Vytautas
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