Theoretical Analysis of Single-Molecule Force Spectroscopy Experiments: Heterogeneity of Chemical Bonds

Raible, Martin; Evstigneev, Mykhaylo; Bartels, Frank Wilco; Eckel, Rainer; Nguyen-Duong, M.; Merkel, Rudolf; Ros, Robert; Anselmetti, Dario; Reimann, Peter

doi:10.1529/biophysj.105.077099

Cited by 69 publications

(129 citation statements)

References 32 publications

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“…Recently, it has been proposed that deviations in rupture force histograms from the DFS predictions are caused by an intrinsic heterogeneity of bond parameters [28]. The increased width and large force tails could be described imposing Gaussian noise on F 0 .…”

Section: Discussionmentioning

confidence: 99%

Dynamic force spectroscopy on multiple bonds: Experiments and model

et al. 2008

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We probe the dynamic strength of multiple biotin-streptavidin adhesion bonds under linear loading using the biomembrane force probe setup for dynamic force spectroscopy. Measured rupture force histograms are compared to results from a master equation model for the stochastic dynamics of bond rupture under load. This allows us to extract the distribution of the number of initially closed bonds. We also extract the molecular parameters of the adhesion bonds, in good agreement with earlier results from single bond experiments. Our analysis shows that the peaks in the measured histograms are not simple multiples of the single bond values, but follow from a superposition procedure which generates different peak positions.

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Section: Discussionmentioning

confidence: 99%

Dynamic force spectroscopy on multiple bonds: Experiments and model

et al. 2008

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“…Thus, it was shown at the single bond level that ligand-receptor couples such as antigen-antibody (Pierres et al, 1995), Streptavidin-biotin , integrin-fibronectin (Vitte et al, 2004a) or C-cadherin/C-cadherin (Pierres et al, 2007) could display a series of binding states with different lifetimes. As will be discussed below, this situation accounts for a variety of results that have been formulated in different ways such as dependence of rupture on bond history (Pincet et al, 2005 ;Marshall et al, 2005) or bond heterogeneity (Raible et al, 2006). Also, this imposes a tremendous complexity on the concept and experimental determination of association rates.…”

Section: Results Obtained With Flow Chambersmentioning

confidence: 99%

What is the biological relevance of the specific bond properties revealed by single‐molecule studies?

Robert

Benoliel

Pierrès

et al. 2007

J of Molecular Recognition

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During the last decade, many authors took advantage of new methodologies based on atomic force microscopy (AFM), biomembrane force probes (BFPs), laminar flow chambers or optical traps to study at the single‐molecule level the formation and dissociation of bonds between receptors and ligands attached to surfaces. Experiments provided a wealth of data revealing the complexity of bond response to mechanical forces and the dependence of bond rupture on bond history. These results supported the existence of multiple binding states and/or reaction pathways. Also, single bond studies allowed us to monitor attachments mediated by a few bonds. The aim of this review is to discuss the impact of this new information on our understanding of biological molecules and phenomena. The following points are discussed: (i) which parameters do we need to know in order to predict the behaviour of an encounter between receptors and ligands, (ii) which information is actually yielded by single‐molecule studies and (iii) is it possible to relate this information to molecular structure? Copyright © 2007 John Wiley & Sons, Ltd.

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“…In some cases, a long tail of the distribution towards higher forces was observed (Figure 4). This tail has been attributed to diverse causes such as heterogeneity of chemical bonds [30] or simultaneous ruptures of more than one complex [31,32]. A plot of the most probable rupture force vs. the most probable loading rate at each retracting speed is shown in Figure 5.…”

Section: Figurementioning

confidence: 99%