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Biophys J, June 2002, p. 3214-3223, Vol. 82, No. 6
Laboratoire d'Immunologie, INSERM U 387, Hôpital Ste-Marguerite, BP 29, 13274 Marseille Cedex 09, France
A laminar flow chamber was used to study single molecule
interactions between biotinylated surfaces and streptavidin-coated spheres subjected to a hydrodynamic drag lower than a piconewton. Spheres were tracked with 20 ms and 40 nm resolution. They displayed multiple arrests lasting between a few tens of milliseconds and several
minutes or more. Analysis of about 500,000 positions revealed that
streptavidin-biotin interaction was multiphasic: transient bound states
displayed a rupture frequency of 5.3 s
1 and a rate of
transition toward a more stable configuration of 1.3 s1.
These parameters did not display any significant change when the force
exerted on bonds varied between 3.5 and 11 pN. However, the apparent
rate of streptavidin-biotin association exhibited about 10-fold
decrease when the wall shear rate was increased from 7 to 22 s1, which supports the existence of an energy barrier
opposing the formation of the transient binding state. It is concluded
that a laminar flow chamber can yield new and useful information on the
formation of molecular bonds, and especially on the structure of the
external part of the energy landscape of ligand-receptor complexes.
Biophys J, June 2002, p. 3214-3223, Vol. 82, No. 6
© 2002 by the Biophysical Society 0006-3495/02/06/3214/10 $2.00
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