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Elastic Modulus Mapping
This publication focuses on utilizing the Agilent 7500 Atomic Force Microscope (AFM) for mapping the elastic modulus of biological cells, with a specific emphasis on endothelial cells. AFM force-distance curves enable quantitative measurement of cell elasticity at nanoscale resolution, providing insights into cellular processes such as migration, division, and growth. Elastic modulus mapping is achieved by acquiring two-dimensional arrays of force-distance curves, which are analyzed using the Hertzian contact mechanics model.
The study demonstrates that cell elasticity is influenced by factors such as actin cytoskeleton organization and nuclear morphology. Elasticity measurements revealed that flat cell regions are stiffer compared to areas around the nucleus. The method also highlights the potential of AFM in biomedical applications, such as distinguishing between cancerous and benign cells based on their nanomechanical properties. This approach provides high-resolution insights into cell mechanics, advancing the understanding of dynamic cellular behaviors and their responses to drugs.
Force Spectroscopy with the Atomic Force Microscope
This publication explores force spectroscopy using Atomic Force Microscopy (AFM) as a powerful technique for measuring nanoscale forces and characterizing molecular interactions. AFM force spectroscopy enables the study of tip-sample interactions by deactivating the feedback loop, allowing precise measurements of forces as small as picoNewtons. It has diverse applications across biology, chemistry, and materials science, particularly in analyzing intermolecular and intramolecular forces.
Key methodologies include functionalized AFM tips for specific molecular interactions and nanoindentation techniques for assessing surface mechanical properties. The study highlights the use of the Thermal Tune method for calibrating cantilever spring constants, enhancing the accuracy of force measurements. Applications such as protein unfolding (e.g., Titin), adhesion studies, and long-range attractive force measurements demonstrate the technique’s versatility.
The integration of advanced features like volume spectroscopy, custom spectroscopy controls, and statistical data analysis further broadens AFM’s applicability. This approach offers critical insights for advancing nanotechnology and understanding molecular-scale phenomena.
Using Thermal K to Calibrate the Spring Constants (k) of AFM Probes
This publication introduces the Thermal K method for calibrating the spring constants (k) of atomic force microscopy (AFM) probes, a critical parameter for accurate force measurements in AFM applications. The spring constant reflects the cantilever’s sensitivity to force and is essential for quantifying material compliance and molecular interactions at the picoNewton scale.
Thermal K leverages the equipartition theorem, treating the cantilever as a harmonic oscillator. It uses the thermal noise and the resonant peak in the Power Spectral Density (PSD) plot to determine the spring constant. The method involves calibrating cantilever deflection sensitivity by obtaining deflection-distance curves and using a rigid substrate like mica.
This technique overcomes variability in nominal spring constants due to manufacturing inconsistencies, providing precise, empirical values for each cantilever. Thermal K ensures reliable measurements in AFM studies, enabling detailed investigations of material properties and molecular mechanics at nanoscale resolution.