ArticleProceedings of the National Academy of Sciences of the United States of America1999
Direct observation of the anchoring process during the adsorption of fibrinogen on a solid surface by force-spectroscopy mode atomic force microscopy.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Atomic force microscopy studies of the initial interactions between fibrinogen and surfaces.Langmuir : the ACS journal of surfaces and colloids · 2009Article
- Innovation focus: the patient with arrhythmia.Journal of cardiovascular translational research · 2008Article
- AFM of biological complexes: what can we learn?Current opinion in colloid & interface science · 2008Article
- Effects of surface wettability and contact time on protein adhesion to biomaterial surfaces.Biomaterials · 2007Article
- Multifunctional polyelectrolyte multilayer films: combining mechanical resistance, biodegradability, and bioactivity.Biomacromolecules · 2007Article
- Multi-bead-and-spring model to interpret protein detachment studied by AFM force spectroscopy.Biophysical journal · 2002Article
- Dissecting streptavidin-biotin interaction with a laminar flow chamber.Biophysical journal · 2002Article
- Unbinding process of adsorbed proteins under external stress studied by atomic force microscopy spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2000Article
Corrections and comments
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Authors and funding
7 authors.
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Abstract
Atomic force microscopy in a force-spectroscopy mode has been used to investigate the kinetics of the adsorption process of fibrinogen molecules on a silica surface. An original "approach/retraction" cycle of the tip/surface was used for this purpose. Fibrinogen molecules were adsorbed on the atomic force microscopy tip and were brought into contact with the silica surface for different interaction times varying from 5 to 2,000 ms. Multiple consecutive ruptures were observed. The mean number of ruptures nr per cycle increases steadily with the interaction time as well as the mean strength fr which varies from 300 pN for 5 ms to 1,400 pN for 2,000 ms. The minimal interaction time for a fibrinogen molecule to bind strongly to a silica surface during an adsorption process appears to lie between 50 and 200 ms. The histograms of the distances between two consecutive ruptures in one cycle exhibit maxima around 20-25 nm. This length is comparable to the characteristic distance between D and E globules of one fibrinogen molecule and suggests that fibrinogen molecules mainly adsorb through their D and E globules.
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