Version 1
: Received: 29 September 2024 / Approved: 30 September 2024 / Online: 30 September 2024 (12:45:56 CEST)
How to cite:
Jankowska, E.; Witkowska, J.; Wityk, P.; Pilarski, M.; Skibiszewska, S. Inhibition of Serum Amyloid A Protein Aggregation by a Five-Residue Peptidomimetic: Structural and Morphological Insights. Preprints2024, 2024092366. https://doi.org/10.20944/preprints202409.2366.v1
Jankowska, E.; Witkowska, J.; Wityk, P.; Pilarski, M.; Skibiszewska, S. Inhibition of Serum Amyloid A Protein Aggregation by a Five-Residue Peptidomimetic: Structural and Morphological Insights. Preprints 2024, 2024092366. https://doi.org/10.20944/preprints202409.2366.v1
Jankowska, E.; Witkowska, J.; Wityk, P.; Pilarski, M.; Skibiszewska, S. Inhibition of Serum Amyloid A Protein Aggregation by a Five-Residue Peptidomimetic: Structural and Morphological Insights. Preprints2024, 2024092366. https://doi.org/10.20944/preprints202409.2366.v1
APA Style
Jankowska, E., Witkowska, J., Wityk, P., Pilarski, M., & Skibiszewska, S. (2024). Inhibition of Serum Amyloid A Protein Aggregation by a Five-Residue Peptidomimetic: Structural and Morphological Insights. Preprints. https://doi.org/10.20944/preprints202409.2366.v1
Chicago/Turabian Style
Jankowska, E., Marcel Pilarski and Sandra Skibiszewska. 2024 "Inhibition of Serum Amyloid A Protein Aggregation by a Five-Residue Peptidomimetic: Structural and Morphological Insights" Preprints. https://doi.org/10.20944/preprints202409.2366.v1
Abstract
Serum amyloid A (SAA) is a small, consisting of 104 residues, protein, which under physiological conditions exists mainly in hexameric form. It belongs to the positive acute-phase proteins, which means that its plasma concentration increases rapidly in response to injury, inflammation, and infection. The accumulation of SAA molecules promotes the formation of amyloid aggregates, which deposit extracellularly in many organs, causing their dysfunction. In our previous work, we successfully designed a peptidomimetic that inhibited the aggregation of amyloidogenic SAA fragments. In the present paper, we show how the same inhibitor, named saa3Dip, affects oligomerization and aggregation processes of MetSAA1.1 protein. The Thioflavin T assay showed that saa3Dip inhibits its fibrillization. The measurement of the internal fluorophore fluorescence (Trp) showed differences that occur in the tertiary structure of MetSAA1.1 in the presence of the inhibitor, which was also confirmed by CD spectra in the aromatic range. FTIR results suggested that saa3Dip can stabilize some fragments of the native structure of MetSAA1.1, which was confirmed by determining the melting temperature (Tm) of the protein-inhibitor complex. AFM images demonstrated that the presence of saa3Dip prevents the formation of large SAA aggregates. Our results suggest that saa3Dip stabilizes the native conformation of MetSAA1.1.
Keywords
Serum Amyloid A; aggregation; inhibitor
Subject
Biology and Life Sciences, Life Sciences
Copyright:
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
