Theoretical analysis of dynamic force spectroscopy experiments on ligand-receptor complexes

Raible M, Evstigneev M, Reimann P, Bartels FW, Ros R (2004)
Journal of Biotechnology 112(1-2): 13-23.

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The forced rupture of single chemical bonds in biomolecular compounds (e.g. ligand-receptor systems) as observed in dynamic force spectroscopy experiments is addressed. Under the assumption that the probability of bond rupture depends only on the instantaneously acting force, a data collapse onto a single master curve is predicted. For rupture data obtained experimentally by dynamic AFM force spectroscopy of a ligand-receptor bond between a DNA and a regulatory protein we do not find such a collapse. We conclude that the above mentioned, generally accepted assumption is not satisfied and we discuss possible explanations. (C) 2004 Elsevier B.V. All rights reserved.
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Raible M, Evstigneev M, Reimann P, Bartels FW, Ros R. Theoretical analysis of dynamic force spectroscopy experiments on ligand-receptor complexes. Journal of Biotechnology. 2004;112(1-2):13-23.
Raible, M., Evstigneev, M., Reimann, P., Bartels, F. W., & Ros, R. (2004). Theoretical analysis of dynamic force spectroscopy experiments on ligand-receptor complexes. Journal of Biotechnology, 112(1-2), 13-23. doi:10.1016/j.biotec.2004.04.017
Raible, M., Evstigneev, M., Reimann, P., Bartels, F. W., and Ros, R. (2004). Theoretical analysis of dynamic force spectroscopy experiments on ligand-receptor complexes. Journal of Biotechnology 112, 13-23.
Raible, M., et al., 2004. Theoretical analysis of dynamic force spectroscopy experiments on ligand-receptor complexes. Journal of Biotechnology, 112(1-2), p 13-23.
M. Raible, et al., “Theoretical analysis of dynamic force spectroscopy experiments on ligand-receptor complexes”, Journal of Biotechnology, vol. 112, 2004, pp. 13-23.
Raible, M., Evstigneev, M., Reimann, P., Bartels, F.W., Ros, R.: Theoretical analysis of dynamic force spectroscopy experiments on ligand-receptor complexes. Journal of Biotechnology. 112, 13-23 (2004).
Raible, M, Evstigneev, Mykhaylo, Reimann, Peter, Bartels, FW, and Ros, R. “Theoretical analysis of dynamic force spectroscopy experiments on ligand-receptor complexes”. Journal of Biotechnology 112.1-2 (2004): 13-23.
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Tuning interfacial patterns of molecular bonds via surface morphology.
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PMID: 28869265
Directly measuring single-molecule heterogeneity using force spectroscopy.
Hinczewski M, Hyeon C, Thirumalai D., Proc Natl Acad Sci U S A 113(27), 2016
PMID: 27317744
Single molecular recognition force spectroscopy study of a DNA aptamer with the target epithelial cell adhesion molecule.
Wang N, Liu H, Hao J, Bai X, Li H, Zhang Z, Wang H, Tang J., Analyst 140(18), 2015
PMID: 26229987
Energy Landscape of Alginate-Epimerase Interactions Assessed by Optical Tweezers and Atomic Force Microscopy.
Håti AG, Aachmann FL, Stokke BT, Skjåk-Bræk G, Sletmoen M., PLoS One 10(10), 2015
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Fuhrmann A, Getfert S, Fu Q, Reimann P, Lindsay S, Ros R., Biophys J 102(10), 2012
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PMID: 21190677
Functional characterization of a supramolecular affinity switch at the single molecule level.
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Scaling of the rupture dynamics of polymer chains pulled at one end at a constant rate.
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Quantitative analysis of single-molecule RNA-protein interaction.
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Bond-rupture immunosensors--a review.
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Refined procedure of evaluating experimental single-molecule force spectroscopy data.
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PMID: 17384066
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Force spectroscopy of single multidomain biopolymers: a master equation approach.
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PMID: 16172803

39 References

Data provided by Europe PubMed Central.

Force spectroscopy on single passive biomolecules and single biomolecular bonds
Merkel, Phys. Rep. 346(), 2001

AUTHOR UNKNOWN, 0
Novel approach to atomic force microscopy
Meyer, Appl. Phys. Lett. 53(), 1988
Intermolecular forces and energies between ligands and receptors.
Moy VT, Florin EL, Gaub HE., Science 266(5183), 1994
PMID: 7939660
Surface anchoring reduces the lifetime of single specific bonds
Nguyen-Duong, Europhys. Lett. 61(), 2003
Forces and energetics of hapten-antibody dissociation: a biased molecular dynamics simulation study.
Paci E, Caflisch A, Pluckthun A, Karplus M., J. Mol. Biol. 314(3), 2001
PMID: 11846569
Elastically coupled two-level systems as a model for biopolymer extensibility
Rief, Phys. Rev. Lett. 81(), 1998

AUTHOR UNKNOWN, 0
Unbinding forces of single antibody-antigen complexes correlate with their thermal dissociation rates.
Schwesinger F, Ros R, Strunz T, Anselmetti D, Guntherodt HJ, Honegger A, Jermutus L, Tiefenauer L, Pluckthun A., Proc. Natl. Acad. Sci. U.S.A. 97(18), 2000
PMID: 10963664
Rupture of multiple parallel molecular bonds under dynamic loading.
Seifert U., Phys. Rev. Lett. 84(12), 2000
PMID: 11017316
Escape from a metastable well under a time-ramped force
Shillcock, Phys. Rev. E 57(), 1998
Model energy landscapes and the force-induced dissociation of ligand-receptor bonds.
Strunz T, Oroszlan K, Schumakovitch I, Guntherodt H, Hegner M., Biophys. J. 79(3), 2000
PMID: 10968985

AUTHOR UNKNOWN, 0

AUTHOR UNKNOWN, 0

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