Exactly solvable models of irreversible adsorption with particle spreading

Boyer, Denis; Talbot, J.; Tarjus, Gilles; Tassel, Patrick; Viot, Pascal

doi:10.1103/physreve.49.5525

Cited by 20 publications

(24 citation statements)

References 14 publications

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“…Recently, three one-dimensional models of irreversible adsorption with subsequent transition have been introduced [78]. In each of these, particles are modeled as line segments of initial length σ α that deposit randomly and sequentially onto an infinite line at a rate k a .…”

Section: A One-dimensional Modelsmentioning

confidence: 99%

From car parking to protein adsorption: an overview of sequential adsorption processes

Talbot

Tarjus

Tassel

et al. 2000

Colloids and Surfaces A: Physicochemical and Engineering Aspect

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409

354

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The adsorption or adhesion of large particles (proteins, colloids, cells, . . . ) at the liquid-solid interface plays an important role in many diverse applications. Despite the apparent complexity of the process, two features are particularly important: 1) the adsorption is often irreversible on experimental time scales and 2) the adsorption rate is limited by geometric blockage from previously adsorbed particles. A coarse-grained description that encompasses these two properties is provided by sequential adsorption models whose simplest example is the random sequential adsorption (RSA) process. In this article, we review the theoretical formalism and tools that allow the systematic study of kinetic and structural aspects of these sequential adsorption models. We also show how the reference RSA model may be generalized to account for a variety of experimental features including particle anisotropy, polydispersity, bulk diffusive transport, gravitational effects, surface-induced conformational and orientational change, desorption, and multilayer formation. In all cases, the significant theoretical results are presented and their accuracy (compared to computer simulation) and applicability (compared to experiment) are discussed.

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Section: A One-dimensional Modelsmentioning

confidence: 99%

From car parking to protein adsorption: an overview of sequential adsorption processes

Talbot

Tarjus

Tassel

et al. 2000

Colloids and Surfaces A: Physicochemical and Engineering Aspect

Self Cite

409

354

View full text Add to dashboard Cite

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“…[23][24][25] Particles are modeled as disks of diameter ␣ that adsorb onto a flat surface randomly, sequentially, and without overlap. Following adsorption, a particle either i͒ desorbs from the surface or ii͒ attempts to spread discretely and symmetrically to a larger diameter ␤ .…”

Section: Modelmentioning

confidence: 99%

A kinetic model of partially reversible protein adsorption

Tassel

Viot

Tarjus

1997

The Journal of Chemical Physics

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Determination of fluid-solid transitions in model protein solutions using the histogram reweighting method and expanded ensemble simulations Monte Carlo studies of the thermodynamics and kinetics of reduced protein models: Application to small helical, β, and α/β proteins We present a kinetic adsorption model for proteins that accounts for the experimentally observed properties of partial reversibility and surface induced conformational change. Particles ͑proteins͒ are modeled as disks that adsorb sequentially and without overlap at random positions onto a surface. Following adsorption, a particle can either desorb or spread symmetrically to a larger size. If the latter occurs, it remains adsorbed irreversibly. Both of these events obey first order kinetic rate laws. We derive analytical results in the asymptotic regime and report Monte Carlo results for shorter times. This model yields adsorbed phases that are more dense than those predicted by models of purely irreversible adsorption. We attribute this densification to a fluid structure that is quite liquidlike. We show that a number of experimentally observed kinetic behaviors can be reproduced with this model and that it is in good quantitative agreement with recent experiments.

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“…The unfolding or spreading of protein molecules upon adsorption leads to the exposure of their hydrophobic core. This is a well-known effect observed experimentally (7)(8)(9)(10)(11)(12)(13)(14)(15)(16)(17) and modeled by means of analytical approximations (18,19) or by computer simulations including molecular dynamics (20,21) and Monte Carlo methods (22)(23)(24)(25)(26). A general picture emerging from these studies confirms that the adsorption of proteins on solid surfaces can be viewed as a multistep process that depends strongly on various external parameters such as the temperature, the pH, or the organic-modifier content of the mobile phases used in HPLC.…”

Section: Introductionmentioning

confidence: 98%

True and Apparent Temperature Dependence of Protein Adsorption Equilibrium in Reversed‐Phase HPLC

Szabelski

Cavazzini

Kaczmarski

et al. 2002

Biotechnology Progress

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The adsorption behavior of bovine insulin on a C(8)-bonded silica stationary phase was investigated at different column pressures and temperatures in isocratic reversed-phase HPLC. Changes in the molar volume of insulin (deltaV(m)) upon adsorption were derived from the pressure dependence of the isothermal retention factor (k'). The values of deltaV(m) were found to be practically independent of the temperature between 25 and 50 degrees C at -96 mL/mol and to increase with increasing temperature, up to -108 mL/mol reached at 50 degrees C. This trend was confirmed by two separate series of measurements of the thermal dependence of ln(k'). In the first series the average column pressure was kept constant. The second series involved measurements of ln(k') under constant mobile-phase flow rate, the average column pressure varying with the temperature. In both cases, a parabolic shape relationship was observed between ln(k') and the temperature, but the values obtained for ln k' were higher in the first than in the second case. The relative difference in ln(k'), caused by the change in pressure drop induced by the temperature, is equivalent to a systematic error in the estimate of the Gibbs free energy of 12%. Thus, a substantial error is made in the estimates of the enthalpy and entropy of adsorption when neglecting the pressure effects associated with the change in the molar volume of insulin. This work proves that the average column pressure must be kept constant during thermodynamic measurements of protein adsorption constants, especially in RPLC and HIC. Our results show also that there is a critical temperature, T(c) approximately equals 53 degrees C, at which ln(k') is maximum and the insulin adsorption process changes from an exothermic to an endothermic one. This temperature determines also the transition point in the molecular mechanism of insulin adsorption that involves successive unfolding of the protein chain.

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Exactly solvable models of irreversible adsorption with particle spreading

Cited by 20 publications

References 14 publications

From car parking to protein adsorption: an overview of sequential adsorption processes

From car parking to protein adsorption: an overview of sequential adsorption processes

A kinetic model of partially reversible protein adsorption

True and Apparent Temperature Dependence of Protein Adsorption Equilibrium in Reversed‐Phase HPLC

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