Morphological and Biophysical Study of S100A9 Protein Fibrils by Atomic Force Microscopy Imaging and Nanomechanical Analysis
Year: 2024
Type: article
Abstract: Atomic force microscopy (AFM) imaging enables the visualization of protein molecules with high resolution, providing insights into their shape, size, and surface topography. Here, we use AFM to study the aggregation process of protein S100A9 in physiological conditions, in the presence of calcium at a molar ratio 4Ca2+:S100A9. We find that S100A9 readily assembles into a worm-like fibril, with a period dimension along the fibril axis of 11.5 nm. The fibril’s chain length extends up to 136 periods after an incubation time of 144 h. At room temperature, the fibril’s bending stiffness was found to be 2.95×10−28 Nm2, indicating that the fibrils are relatively flexible. Additionally, the values obtained for the Young’s modulus (Ex=6.96×105 Pa and Ey=3.37×105 Pa) are four orders of magnitude lower than those typically reported for canonical amyloid fibrils. Our findings suggest that, under the investigated conditions, a distinct aggregation mechanism may be in place in the presence of calcium. Therefore, the findings reported here could have implications for the field of biomedicine, particularly with regard to Alzheimer’s disease.
Source: Biomolecules
DOI: 10.3390/biom14091091
Institutions: University of Lisbon, Instituto Biofisika
Language: English
Topic: S100 Proteins and Annexins
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: gold
Estimated APC paid: $3,069
Awards: Twinning for excellence in biophysics of protein interactions and self-assembly, Instituto de Biosistemas & Ciências Integrativas, G6327780096, G6441380948, Instituto de Biosistemas & Ciências Integrativas, G78871869, Insights into Cystic Fibrosis and Alzheimers disease using Atomic Force Microscopy related techniques
OpenAlex ID: W4402146752