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Pro-Inflammatory S100A9 Protein Aggregation Promoted by NCAM1 Peptide Constructs
Jonathan Pansieri1, Lucija Ostojić1, Igor A Iashchishyn1
1Department of Medical Biochemistry and Biophysics , Umeå University , SE-901 87 Umeå , Sweden.
ACS Chemical Biology
|June 14, 2019
Summary
NCAM1 peptide constructs accelerate S100A9 amyloid self-assembly by catalyzing individual molecule misfolding. This modulation of S100A9 aggregation may offer a novel strategy for tuning the amyloid cascade in neurodegenerative diseases.
Area of Science:
- Neuroscience
- Biochemistry
- Molecular Biology
Background:
- Amyloid cascade and neuroinflammation are key features of neurodegenerative diseases.
- Pro-inflammatory S100A9 protein plays a central role in both processes.
Purpose of the Study:
- To investigate the effect of NCAM1 peptide constructs on S100A9 amyloid self-assembly.
- To explore the potential of modulating S100A9 aggregation for therapeutic strategies.
Main Methods:
- Utilized NCAM1 peptide constructs with polycationic sequences from Aβ and PrP.
- Studied the concentration-dependent effects of these constructs on S100A9 self-assembly.
- Investigated the mechanism involving transient interactions and perturbation of native S100A9 structure.
Main Results:
- NCAM1 peptide constructs significantly promoted S100A9 amyloid self-assembly in a concentration-dependent manner.
- These constructs acted as catalysts by interacting with individual S100A9 molecules and perturbing their native structure.
- The observed rapid self-assembly into large clumps may inhibit amyloid tissue propagation.
Conclusions:
- NCAM1 peptide constructs effectively catalyze S100A9 amyloid self-assembly, targeting a rate-limiting step in the aggregation process.
- Modulating S100A9 aggregation via these constructs offers a potential method for tuning the amyloid cascade.
- This approach could be relevant for developing therapeutic strategies for neurodegenerative diseases.
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