Direct observation of the anchoring process during the adsorption of fibrinogen on a solid surface by force-spectroscopy mode atomic force microscopy.
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.
Hemmerlé
J
J
Institut National de la Santé et de la Recherche Médicale U424, Fédération de Recherche Odontologie, 11 rue Humann, 67085 Strasbourg Cedex, France. hemmerle@odont3.u-strasbg.fr
Altmann
S M
SM
Maaloum
M
M
Hörber
J K
JK
Heinrich
L
L
Voegel
J C
JC
Schaaf
P
P
D005340:Fibrinogen / Q000737:chemistry*; D006801:Humans; D018625:Microscopy, Atomic Force; D011485:Protein Binding; D011487:Protein Conformation
D005340:Fibrinogen