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.
Bibliography
Gergely, C., Voegel, J.-C., Schaaf, P., Senger, B., Maaloum, M., Hörber, J. K. H., & Hemmerlé, J. (2000). Unbinding process of adsorbed proteins under external stress studied by atomic force microscopy spectroscopy. Proceedings of the National Academy of Sciences, 97(20), 10802â10807.
References
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Dates
Type | When |
---|---|
Created | 23 years, 1 month ago (July 26, 2002, 10:41 a.m.) |
Deposited | 3 years, 4 months ago (April 13, 2022, 4:07 a.m.) |
Indexed | 1 year, 10 months ago (Oct. 9, 2023, 2:47 p.m.) |
Issued | 24 years, 11 months ago (Sept. 12, 2000) |
Published | 24 years, 11 months ago (Sept. 12, 2000) |
Published Online | 24 years, 11 months ago (Sept. 12, 2000) |
Published Print | 24 years, 11 months ago (Sept. 26, 2000) |
@article{Gergely_2000, title={Unbinding process of adsorbed proteins under external stress studied by atomic force microscopy spectroscopy}, volume={97}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.180293097}, DOI={10.1073/pnas.180293097}, number={20}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Gergely, C. and Voegel, J.-C. and Schaaf, P. and Senger, B. and Maaloum, M. and Hörber, J. K. H. and Hemmerlé, J.}, year={2000}, month=sep, pages={10802–10807} }