Measuring the kinetics of biomolecular recognition with magnetic colloids.
We introduce a general methodology based on magnetic colloids to study the recognition kinetics of tethered biomolecules. Access to the full kinetics of the reaction is provided by an explicit measure of the time evolution of the reactant densities. Binding between a single ligand and its complementary receptor is here limited by the colloidal rotational diffusion. It occurs within a binding distance that can be extracted by a reaction-diffusion theory that properly accounts for the rotational Brownian dynamics. Our reaction geometry allows us to probe a large diversity of bioadhesive molecules and tethers, thus providing a quantitative guidance for designing more efficient reactive biomimetic surfaces, as required for diagnostic, therapeutic, and tissue engineering techniques.
Cohen-Tannoudji
L
L
ESPCI, UMR 7612, Laboratoire Colloïdes et Matériaux Divisés, ParisTech, 10 rue Vauquelin, Paris, F-75005 France.
Bertrand
E
E
Baudry
J
J
Robic
C
C
Goubault
C
C
Pellissier
M
M
Johner
A
A
Thalmann
F
F
Lee
N K
NK
Marques
C M
CM
Bibette
J
J
D001710:Biotin / Q000737:chemistry; D003102:Colloids / Q000737:chemistry*; D007700:Kinetics; D008280:Magnetics; D011956:Receptors, Cell Surface / Q000032:analysis*; D012710:Serum Albumin, Bovine / Q000737:chemistry; D019809:Streptavidin / Q000737:chemistry
D003102:Colloids; D011956:Receptors, Cell Surface; D012710:Serum Albumin, Bovine; D001710:Biotin; D019809:Streptavidin