Morphological and Biophysical Study of S100A9 Protein Fibrils by Atomic Force Microscopy Imaging and Nanomechanical Analysis
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...
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| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2024-08-01
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| Series: | Biomolecules |
| Subjects: | |
| Online Access: | https://www.mdpi.com/2218-273X/14/9/1091 |
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| Summary: | 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 4Ca<sup>2+</sup>: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 <inline-formula><math xmlns="http://www.w3.org/1998/Math/MathML" display="inline"><semantics><mrow><mn>2.95</mn><mo>×</mo><msup><mn>10</mn><mrow><mo>−</mo><mn>28</mn></mrow></msup></mrow></semantics></math></inline-formula> Nm<sup>2</sup>, indicating that the fibrils are relatively flexible. Additionally, the values obtained for the Young’s modulus (<inline-formula><math xmlns="http://www.w3.org/1998/Math/MathML" display="inline"><semantics><mrow><msub><mi>E</mi><mi>x</mi></msub><mo>=</mo><mn>6.96</mn><mo>×</mo><msup><mn>10</mn><mn>5</mn></msup></mrow></semantics></math></inline-formula> Pa and <inline-formula><math xmlns="http://www.w3.org/1998/Math/MathML" display="inline"><semantics><mrow><msub><mi>E</mi><mi>y</mi></msub><mo>=</mo><mn>3.37</mn><mo>×</mo><msup><mn>10</mn><mn>5</mn></msup></mrow></semantics></math></inline-formula> 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. |
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| ISSN: | 2218-273X |