Single Molecule Force Spectroscopy on Polysaccharides by Atomic Force Microscopy

Rief, Matthias; Oesterhelt, Filipp; Heymann, Berthold; Gaub, Hermann E.

doi:10.1126/science.275.5304.1295

Cited by 1,097 publications

(985 citation statements)

References 9 publications

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“…This structural modification was correlated with a change of molecular interactions; while dormant spores showed poor adhesion, germinating spores showed large attractive forces, along with elongation forces that were attributed to the stretching of single cell surface polysaccharides. This interpretation was supported by the finding that fitting the curves with a theoretical model from statistical mechanics yielded parameters similar to those reported for individual amylose and dextran molecules (Rief et al, 1997). It was concluded that the stickiness and flexibility of cell surface polysaccharide chains may promote spore aggregation via macromolecular bridging interactions between opposing cells.…”

Section: Imaging Living Cells and Following Dynamic Processessupporting

confidence: 65%

“…AFM has also proved very useful to probe intramolecular forces associated with single poly- saccharides and proteins, thereby providing quantitative information on their elasticity, on conformational transitions along the chains and on folding/unfolding forces (Rief et al, 1997;Oesterhelt et al, 2000). In a mycological context, AFM was used to pull on macromolecules exposed at the surface of living A. oryzae spores, with the aim of gaining insight into their elasticity ( Figure 6; van der Aa et al, 2001).…”

Section: Imaging Living Cells and Following Dynamic Processesmentioning

confidence: 99%

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Towards a nanoscale view of fungal surfaces

Dague

Gilbert

Verbelen

et al. 2007

Yeast

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In the past years, atomic force microscopy (AFM) has offered novel possibilities for exploring the nanoscale surface properties of fungal cells. For the first time, AFM imaging enables investigators to visualize fine surface structures, such as rodlets, directly on native hydrated cells. Moreover, real-time imaging can be used to follow cell surface dynamics during cell growth and to monitor the effect of molecules such as enzymes and drugs. In fact, AFM is much more than a microscope in that when used in the force spectroscopy mode, it allows measurement of physicochemical properties such as surface energy and surface charge, to probe the elasticity of cell wall components and macromolecules, and to analyse the force and localization of molecular recognition events.

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Section: Imaging Living Cells and Following Dynamic Processessupporting

confidence: 65%

Section: Imaging Living Cells and Following Dynamic Processesmentioning

confidence: 99%

Towards a nanoscale view of fungal surfaces

Dague

Gilbert

Verbelen

et al. 2007

Yeast

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show abstract

“…1. As described elsewhere, 14,18,[30][31][32][33] the characteristic plateau at 0.3 nN, which is caused by the chair-boat transition of CMA, can be used to confirm that a single molecule has been stretched. At the end of the plateau in Fig.…”

Section: Resultsmentioning

confidence: 99%

Mechanically activated rupture of single covalent bonds: evidence of force induced bond hydrolysis

Schmidt

Kersch

Beyer

et al. 2011

Phys. Chem. Chem. Phys.

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We have used temperature-dependent single molecule force spectroscopy to stretch covalently anchored carboxymethylated amylose (CMA) polymers attached to an amino-functionalized AFM cantilever. Using an Arrhenius kinetics model based on a Morse potential as a one-dimensional representation of covalent bonds, we have extracted kinetic and structural parameters of the bond rupture process. With 35.5 kJ mol À1 , we found a significantly smaller dissociation energy and with 9.0 Â 10 2 s À1 to 3.6 Â 10 3 s À1 also smaller Arrhenius pre-factors than expected for homolytic bond scission. One possible explanation for the severely reduced dissociation energy and Arrhenius pre-factors is the mechanically activated hydrolysis of covalent bonds. Both the carboxylic acid amide and the siloxane bond in the amino-silane surface linker are in principle prone to bond hydrolysis. Scattering, slope and curvature of the scattered data plots indicate that in fact two competing rupture mechanisms are observed.

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“…Dextran and I27 protein molecules were chosen for these starting experiments because both of these molecules can be regarded as standard (if not calibrating) samples for single-molecule force spectroscopy, and have been widely studied (see, e.g., (8,13,18,19,(23)(24)(25)(26)(27)(28)(29)(30)). The dissipative properties of both of these molecules have been described elsewhere (8,13).…”

Section: Materials and Materialsmentioning

confidence: 99%

Can Dissipative Properties of Single Molecules Be Extracted from a Force Spectroscopy Experiment?

Benedetti

Gazizova

Kulik

et al. 2016

Biophysical Journal

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We performed dynamic force spectroscopy of single dextran and titin I27 molecules using small-amplitude and low-frequency (40-240 Hz) dithering of an atomic force microscope tip excited by a sine wave voltage fed onto the tip-carrying piezo. We show that for such low-frequency dithering experiments, recorded phase information can be unambiguously interpreted within the framework of a transparent theoretical model that starts from a well-known partial differential equation to describe the dithering of an atomic force microscope cantilever and a single molecule attached to its end system, uses an appropriate set of initial and boundary conditions, and does not exploit any implicit suggestions. We conclude that the observed phase (dissipation) signal is due completely to the dissipation related to the dithering of the cantilever itself (i.e., to the change of boundary conditions in the course of stretching). For both cases, only the upper bound of the dissipation of a single molecule has been established as not exceeding 3,10 À7 kg=s. We compare our results with previously reported measurements of the viscoelastic properties of single molecules, and we emphasize that extreme caution must be taken in distinguishing between the dissipation related to the stretched molecule and the dissipation that originates from the viscous damping of the dithered cantilever. We also present the results of an amplitude channel data analysis, which reveal that the typical values of the spring constant of a I27 molecule at the moment of module unfolding are equal to 451:5 mN=m, and the typical values of the spring constant of dextran at the moment of chair-boat transition are equal to 30 À 50 mN=m.

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Single Molecule Force Spectroscopy on Polysaccharides by Atomic Force Microscopy

Cited by 1,097 publications

References 9 publications

Towards a nanoscale view of fungal surfaces

Towards a nanoscale view of fungal surfaces

Mechanically activated rupture of single covalent bonds: evidence of force induced bond hydrolysis

Can Dissipative Properties of Single Molecules Be Extracted from a Force Spectroscopy Experiment?

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