Elsevier, Biophysical Journal, 12(105), p. 2771-2780, 2013
DOI: 10.1016/j.bpj.2013.10.030
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Dynamic force spectroscopy was used to test force-induced dissociation of the complex between the integrin α 7 β 1 and the bacterial protein invasin. Both proteins were used in truncated forms comprising the respective binding sites. Using the biomembrane force-probe, the bond system was exposed to 14 different loading rates ranging from 18 pN/s to 5.3 nN/s. At each rate, bond rupture spectra were collected. Median forces ranged from 8 to 72 pN. These showed two linear regimes when plotted against the logarithm of the force-loading rate. However, a statistical analysis of the full rupture force spectra including the detection limits of the setup showed that all measured data are well described by dissociation over a single barrier. © 2013 Biophysical Society.