1. S100A9 inhibits and redirects prion protein 89-230 fragment amyloid aggregation.
- Author
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Ziaunys M, Sulskis D, Mikalauskaite K, Sakalauskas A, Snieckute R, and Smirnovas V
- Subjects
- Animals, Mice, Peptide Fragments metabolism, Peptide Fragments chemistry, Kinetics, Calgranulin B metabolism, Calgranulin B chemistry, Prion Proteins chemistry, Prion Proteins metabolism, Amyloid metabolism, Amyloid chemistry, Protein Aggregates
- Abstract
Protein aggregation in the form of amyloid fibrils has long been associated with the onset and development of various amyloidoses, including Alzheimer's, Parkinson's or prion diseases. Recent studies of their fibril formation process have revealed that amyloidogenic protein cross-interactions may impact aggregation pathways and kinetic parameters, as well as the structure of the resulting aggregates. Despite a growing number of reports exploring this type of interaction, they only cover just a small number of possible amyloidogenic protein pairings. One such pair is between two neurodegeneration-associated proteins: the pro-inflammatory S100A9 and prion protein, which are known to co-localize in vivo. In this study, we examined their cross-interaction in vitro and discovered that the fibrillar form of S100A9 modulated the aggregation pathway of mouse prion protein 89-230 fragment, while non-aggregated S100A9 also significantly inhibited its primary nucleation process. These results complement previous observations of the pro-inflammatory protein's role in amyloid aggregation and highlight its potential role against neurodegenerative disorders., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier Inc. All rights reserved.)
- Published
- 2024
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