Mechanisms of Fibrinogen Adsorption at Solid Substrates

Abstract

Adsorption of fibrinogen, modeled as a linear chain of touching beads of various sizes, was theoretically studied using the random sequential adsorption (RSA) model. The adsorption process was assumed to consist of two steps: (i) formation of an irreversibly bound fibrinogen monolayer under the side-on orientation, which is independent of the bulk protein concentration and (ii) formation of the reversibly bound, end-on monolayer, whose coverage was dependent on the bulk concentration. Calculation based on the RSA model showed that the maximum surface concentration of the end-on (reversible) monolayer equals N(⊥∞) = 6.13 × 10(3) μm(-2) which is much larger than the previously found value for the side-on (irreversible) monolayer, equal to N(∞) = 2.27 × 10(3) μm(-2). Hence, the maximum surface concentration of fibrinogen in both orientations is determined to be 8.40 × 10(3) μm(-2) corresponding to the protein coverage of 5.70 mg m(-2) assuming 20% hydration. Additionally, the surface blocking function (ASF) was determined for the end-on fibrinogen adsorption, approximated for the entire range of coverage by the interpolating polynomial. For the coverage approaching the jamming limit, the surface blocking function (ASF) was shown to vanish proportionally to (θ(⊥∞) - θ(⊥))(2). These calculation allowed one to theoretically predict adsorption isotherms for the end-on regime of fibrinogen and adsorption kinetics under various transport conditions (diffusion and convection). Using these theoretical results, a quantitative interpretation of experimental data obtained by TIRF and ellipsometry was successfully performed. The equilibrium adsorption constant for the end-on adsorption regime was found to be 8.04 × 10(-3) m. On the basis of this value, the depth of the adsorption energy minimum, equal to -17.4 kT, was predicted, which corresponds to ΔG = -41.8 kJ mol(-1). This is in accordance with adsorption energy derived as the sum of the van der Waals and electrostatic interactions. Besides having significance for predicting fibrinogen adsorption, theoretical results derived in this work also have implications for basic science providing information on mechanisms of anisotropic protein molecule adsorption on heterogeneous surfaces.

Mechanisms of fibrinogen adsorption at the silica substrate determined by QCM-D measurements

“…This effect is physically due to the overlapping of the water 'atmospheres' surrounding each molecule. This phenomenon is analogous to the overlapping of exclusion areas (volumes) of adsorbed molecules pertinent to the random sequential adsorption model [40][41][42] and was interpreted along this line by Bingen et al [23] using various hydration models.…”

“…7 were theoretically interpreted in terms of the extended random sequential adsorption model developed in Refs. [40][41][42]. This is an universal approach that allows one to theoretically predict the blocking function and the maximum coverage for various adsorption mechanisms of fibrinogen molecules.…”

“…[40] the limiting case of the purely side-on adsorption mechanism was considered and in Ref. [41] the side-on and afterward end-on mechanism was evaluated. Additionally, in Ref.…”

Properties of random sequential adsorption of generalized dimers

“…In recent studies RSA has also been successfully used for modeling complex particles using coarse-grain approximation [8][9][10][11]. For example, a coarse-grain fibrinogen model successfully explains the density of adsorbed proteins for a wide range of experimental conditions [12][13][14].…”

KfrA plasmid protein monolayers on latex particles-electrokinetic measurements

“…For thinner double layers, where κa > 1, C o i , C o p attain constant values of 10.2 and 6.5, respectively [ 29 ].…”