Kinetics of Desorption of Proteins from the Surface of Protein-Coated Alumina by Various Desorbing Reagents

Sarkar, Deepa; Chattoraj, D. K.

doi:10.1006/jcis.1996.0157

Cited by 36 publications

(19 citation statements)

References 5 publications

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“…It was also shown that k f was influenced by θ, whereas k s was independent on θ. Only a few studies have so far been reported concerning the analysis of desorption curves based on the concept of two types of adsorbates (15,(20)(21)(22). Although it is difficult to compare the rate constants reported in the literature with the values obtained in this study because elution conditions differ largely from each other, some phenomena identical to the results of this study were observed.…”

Section: Discussionsupporting

confidence: 56%

“…The evidence for the distribution in the binding strength of the same protein adsorbed on a solid surface has been obtained indirectly through the degree of irreversibility upon dilution or buffer rinse (8,9), changes in pH and ionic strength (10)(11)(12), and addition of displacers (12)(13)(14). Furthermore, Sarkar and Chattoraj (15) reported that the desorption processes of irreversibly adsorbed proteins on alumina (Al 2 O 3 ) by various desorbing reagents contained two kinetic steps with different rates. They suggested that there exists broadly two types of conformations of the same protein on Al 2 O 3 surfaces.…”

Section: Introductionmentioning

confidence: 97%

See 1 more Smart Citation

Kinetic Study of Desorption of Two Species of Bovine Serum Albumin from Alumina during Alkali Elution Process

Urano

Fukuzaki

2002

Journal of Colloid and Interface Science

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Section: Discussionsupporting

confidence: 56%

Section: Introductionmentioning

confidence: 97%

Kinetic Study of Desorption of Two Species of Bovine Serum Albumin from Alumina during Alkali Elution Process

Urano

Fukuzaki

2002

Journal of Colloid and Interface Science

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“…In this case, desorption kinetics are expected to follow equation 2, which is valid only if readsorption of protein to the interface can be neglected. However, in practice, even if the bulk solution is presented with a large volume per area of interface such that the average protein concentration is negligible after desorption, [59] a significant concentration boundary layer will be established that permits readsorption and alters the apparent desorption kinetics. The effect of the concentration boundary layer can be minimized using flow to remove desorbed protein.…”

Section: Basic Models Of Protein Monolayer Formationmentioning

confidence: 99%

A bottom-up approach to understanding protein layer formation at solid–liquid interfaces

Kastantin

Langdon

Schwartz

2014

Advances in Colloid and Interface Science

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A common goal across different fields (e.g. separations, biosensors, biomaterials, pharmaceuticals) is to understand how protein behavior at solid-liquid interfaces is affected by environmental conditions. Temperature, pH, ionic strength, and the chemical and physical properties of the solid surface, among many factors, can control microscopic protein dynamics (e.g. adsorption, desorption, diffusion, aggregation) that contribute to macroscopic properties like time-dependent total protein surface coverage and protein structure. These relationships are typically studied through a top-down approach in which macroscopic observations are explained using analytical models that are based upon reasonable, but not universally true, simplifying assumptions about microscopic protein dynamics. Conclusions connecting microscopic dynamics to environmental factors can be heavily biased by potentially incorrect assumptions. In contrast, more complicated models avoid several of the common assumptions but require many parameters that have overlapping effects on predictions of macroscopic, average protein properties. Consequently, these models are poorly suited for the top-down approach. Because the sophistication incorporated into these models may ultimately prove essential to understanding interfacial protein behavior, this article proposes a bottom-up approach in which direct observations of microscopic protein dynamics specify parameters in complicated models, which then generate macroscopic predictions to compare with experiment. In this framework, single-molecule tracking has proven capable of making direct measurements of microscopic protein dynamics, but must be complemented by modeling to combine and extrapolate many independent microscopic observations to the macro-scale. The bottom-up approach is expected to better connect environmental factors to macroscopic protein behavior, thereby guiding rational choices that promote desirable protein behaviors.

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“…Of these, K d may be the most straightforward as accurate methods exist to measure the experimental rate of desorption upon dilution of the bulk phase. 29 For more rigid proteins where orientational rather than conformational changes are expected, ⌺ may be estimated by the ratio of the largest to smallest dimension. This is what we have done in modeling the adsorption of lysozyme in Fig.…”

Section: Figmentioning

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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Kinetics of Desorption of Proteins from the Surface of Protein-Coated Alumina by Various Desorbing Reagents

Cited by 36 publications

References 5 publications

Kinetic Study of Desorption of Two Species of Bovine Serum Albumin from Alumina during Alkali Elution Process

Kinetic Study of Desorption of Two Species of Bovine Serum Albumin from Alumina during Alkali Elution Process

A bottom-up approach to understanding protein layer formation at solid–liquid interfaces

A kinetic model of partially reversible protein adsorption

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