ArticleProceedings of the National Academy of Sciences of the United States of America2000
Unbinding process of adsorbed proteins under external stress studied by atomic force microscopy spectroscopy.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed.
- Synchronized motion of interface residues for evaluating protein-RNA complex binding affinity: Application to aptamer-mediated inhibition of TDP-43 aggregates.Protein science : a publication of the Protein Society · 2024Article
- Improving dental epithelial junction on dental implants with bioengineered peptides.Frontiers in bioengineering and biotechnology · 2023Article
- Probing Mitotic CENP-E Kinesin with the Tethered Cargo Motion Assay and Laser Tweezers.Biophysical journal · 2018Article
- Improving estimation of kinetic parameters in dynamic force spectroscopy using cluster analysis.The Journal of chemical physics · 2018Article
- Measuring protein isoelectric points by AFM-based force spectroscopy using trace amounts of sample.Nature nanotechnology · 2016Article
- Highly loaded behavior of kinesins increases the robustness of transport under high resisting loads.PLoS computational biology · 2015Article
- Theory of rapid force spectroscopy.Nature communications · 2014Article
- The influence of inhomogeneous adhesion on the detachment dynamics of adhering cells.European biophysics journal : EBJ · 2013Article
- AFM of biological complexes: what can we learn?Current opinion in colloid & interface science · 2008Article
- Specific bonds between an iron oxide surface and outer membrane cytochromes MtrC and OmcA from Shewanella oneidensis MR-1.Journal of bacteriology · 2007Article
- Probing the interaction between vesicular stomatitis virus and phosphatidylserine.European biophysics journal : EBJ · 2006Article
- Dynamic force spectroscopy of glycoprotein Ib-IX and von Willebrand factor.Biophysical journal · 2005Article
- Kinetics from nonequilibrium single-molecule pulling experiments.Biophysical journal · 2003Article
- Measurement of adhesive forces between individual Staphylococcus aureus MSCRAMMs and protein-coated surfaces by use of optical tweezers.Journal of bacteriology · 2003Article
- Force spectroscopy of the leukocyte function-associated antigen-1/intercellular adhesion molecule-1 interaction.Biophysical journal · 2002Article
- Multi-bead-and-spring model to interpret protein detachment studied by AFM force spectroscopy.Biophysical journal · 2002Article
- Membrane recognition by vesicular stomatitis virus involves enthalpy-driven protein-lipid interactions.Journal of virology · 2002Article
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7 authors.
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Abstract
We report the study of the dynamics of the unbinding process under a force load f of adsorbed proteins (fibrinogen) on a solid surface (hydrophilic silica) by means of atomic force microscopy spectroscopy. By varying the loading rate r(f), defined by f = r(f) t, t being the time, we find that, as for specific interactions, the mean rupture force increases with r(f). This unbinding process is analyzed in the framework of the widely used Bell model. The typical dissociation rate at zero force entering in the model lies between 0. 02 and 0.6 s(-1). Each measured rupture is characterized by a force f(0), which appears to be quantized in integer multiples of 180-200 pN.
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