Probing nanomechanical properties from biomolecules to living cells

Kasas, Sandor; Dietler, Giovanni

doi:10.1007/s00424-008-0448-y

Cited by 90 publications

(70 citation statements)

References 97 publications

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“…The obtained mean Young modulus values were of 0.7 ± 0.5 kPa and 1.2 ± 0.4 kPa, correspondingly (data calculated from Gaussian fit, for the indentation depth of 500 nm). Cell indentation generates the response from inner structural cell components [13]. For small indentations depths the values of the modulus are dominated by the mechanical properties of the cell membrane.…”

Section: Estimation Of the Energy Dissipationmentioning

confidence: 99%

Energy Dissipation in the AFM Elasticity Measurements

et al. 2009

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Nowadays, it is well established that changes of cell stiffness observed by atomic force microscopy are linked with the cell cytoskeleton. Its structural and functional alterations are underlying major diseases such as cancer, inflammation or neurodegenerative disorders. So far, the use of atomic force microscopy is mostly focused on the determination of the Young modulus using the modified Hertz model. It can quantitatively describe the elastic properties of living cells, however, its value is burdened by the fact that cells are neither isotropic nor homogeneous material. Often, during the atomic force microscopy measurements, the hysteresis between the loading and unloading curves are observed which indicates the dissipation of an energy. In our studies, the index of plasticity was introduced to enumerate such effect during a single loading-unloading cycle. As the results show, such approach delivers an additional parameter describing the mechanical state of cell cytoskeleton. The analysis was performed on test samples where the mechanical properties of the melanoma cells were changed by glutaraldehyde and cytochalasin D treatments. The non-treated cells were compared with fibroblasts.

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Section: Estimation Of the Energy Dissipationmentioning

confidence: 99%

Energy Dissipation in the AFM Elasticity Measurements

et al. 2009

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“…Moreover, such measurements can be performed seamlessly in physiological conditions and in presence of different liquid media. This versatility is reflected in the AFM literature which presents with increasing frequency novel results regarding mechanical properties of single cells, bacteria or even single molecules (Berquand et al, 2010;Kasas and Dietler, 2008). At a cellular scale, it has been demonstrated that the mechanical properties of the membrane can reflect the physiological state of the entire system and that these properties are clearly altered in the occurrence of pathological conditions (Cross et al, 2007;Girasole et al, 2010;Lekka et al, 2005).…”

Section: Introductionmentioning

confidence: 99%

Antibiotic-induced modifications of the stiffness of bacterial membranes

Longo

Rio

Trampuž

et al. 2013

Journal of Microbiological Methods

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“…Protein complexes and their network of interactions in cellular function and regulation are at the forefront of biological research [55]. Structural biology methods provide three-dimensional atomic architectures of proteins that provide insights into physiological function, but other factors such as chemical composition, electrical charge distribution, and mechanical properties are also important [56]. Proteins acquire their unique biological functions through folding of their peptides into a unique and stable three-dimensional structure.…”

Section: Mechanically Unfolding Membrane Proteins With Smfsmentioning

confidence: 99%

Progress in measuring biophysical properties of membrane proteins with AFM single-molecule force spectroscopy

Liu

et al. 2014

Chin. Sci. Bull.

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Membrane proteins are crucial in cell physiological activities and are the targets for most drugs. Thus, investigating the behaviors of membrane proteins not only provide deeper insights into cell function, but also help disease treatment and drug development. Atomic force microscopy is a unique tool for investigating the structure of membrane proteins. It can both image the morphology of single native membrane proteins with high resolution and, via single-molecule force spectroscopy (SMFS), directly measure their biophysical properties during molecular physiological activities such as ligand binding and protein unfolding. In the context of molecular biomechanics, SMFS has been successfully used to understand the structure and function of membrane proteins, complementing the static three-dimensional structures of proteins obtained by X-ray crystallography. Here, based on the authors' antigen-antibody binding force measurements in clinical tumor cells, the principle and method of SMFS is discussed, the progress in using SMFS to characterize membrane proteins is summarized, and challenges for SMFS are presented.

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Probing nanomechanical properties from biomolecules to living cells

Cited by 90 publications

References 97 publications

Energy Dissipation in the AFM Elasticity Measurements

Energy Dissipation in the AFM Elasticity Measurements

Antibiotic-induced modifications of the stiffness of bacterial membranes

Progress in measuring biophysical properties of membrane proteins with AFM single-molecule force spectroscopy

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