Flexafm microscope system

Protein amyloid structure formation after the thermal treatment was also confirmed by atomic force microscopy imaging. For this process, 50 µL of protein solution was deposited onto a freshly cleaved mica surface. After 10 min adsorption time, the substrate was gently rinsed in double distilled water and dried in vacuum before imaging in air at room temperature.
Following the QCM adsorption experiments, the dried gold sensor surfaces were also imaged with AFM.
Surface morphology was recorded with a FlexAFM microscope system (Nanosurf AG, Liestal, Switzerland), operating in dynamic mode. Tap150GD-G cantilevers (BudgetSensors Ltd., Sofia, Bulgaria) with a nominal tip radius of less than 10 nm were used for the measurements. Images were recorded over 5 μm × 5 μm window areas at 10 randomly selected locations with a resolution of 512 pixels/line.
Representative line profiles have been extracted from the images to characterize the surface roughness of the samples.

The surface morphology was analyzed using a FlexAFM microscope system (Nanosurf AG, Liestal, Switzerland), operating in dynamic mode controlled by Nanosurf control software C3000 version 3.10.4. The measurements were taken using Tap150GD-G cantilevers (BudgetSensorsLtd., Sofia, Bulgaria), with a nominal tip radius of less than 10 nm. Low-resolution pre-screenings were conducted before data collection to prevent significant height variations in surface topology and identify fibril-like formations. Data collection was performed once from various locations within a single sample. Images were captured in close proximity to optically dense aggregates on the surface, with a window size of 10 µm × 10 µm and a resolution of 512 pixels/line. In several cases, data were collected from the region of interest at a higher resolution. Representative line profiles have been extracted from the images to characterize the cross-section of the filaments. Gwyddion 2.62 software was used to process the AFM data and generate the images.