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Biophys J. 2013 Dec 17;105(12):2771-80. doi: 10.1016/j.bpj.2013.10.030.

Two barriers or not? Dynamic force spectroscopy on the integrin α7β1 invasin complex.

Author information

1
MEMPHYS-Center for Biomembrane Physics, Institute of Physics and Chemistry, University of Southern Denmark, Odense, Denmark.
2
MEMPHYS-Center for Biomembrane Physics, Institute of Physics and Chemistry, University of Southern Denmark, Odense, Denmark; Department of Physics, Jagiellonian University, Cracow, Poland; Institute of Complex Systems 7: Biomechanics, Forschungszentrum Jülich, Jülich, Germany.
3
Institute for Physiological Chemistry and Pathobiochemistry, University of Münster, Münster, Germany.
4
Institute of Complex Systems 7: Biomechanics, Forschungszentrum Jülich, Jülich, Germany.
5
Institute of Complex Systems 7: Biomechanics, Forschungszentrum Jülich, Jülich, Germany. Electronic address: r.merkel@fz-juelich.de.

Abstract

Dynamic force spectroscopy was used to test force-induced dissociation of the complex between the integrin α7β1 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.

PMID:
24359749
PMCID:
PMC3882471
DOI:
10.1016/j.bpj.2013.10.030
[Indexed for MEDLINE]
Free PMC Article
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