Diffusion model of protein adsorption and effect of protein layer composition on water permeability for ultrafiltration membranes

Iordanskii, A. L.; Markin, V. S.; Razumovskii, L.P.; Kosenko, R. Yu.; Tarasova, N. A.; Заиков, Г. Е.

doi:10.1016/0011-9164(96)00033-1

Cited by 7 publications

(4 citation statements)

References 15 publications

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“…Some other studies have assumed that the adsorption kinetics is determined by the diffusion of the proteins to the surface (Iordanskii et al, 1996), whereas others assume that the dominant regime is the one controlled by a kinetic (activated) process (Chatelier and Minton, 1996;Minton, 1999). In a recent study, Cho et al (1997) formulated a model in which both the diffusion and kinetic processes were included.…”

Section: Introductionmentioning

confidence: 99%

Kinetics and Thermodynamics of Protein Adsorption: A Generalized Molecular Theoretical Approach

Fang

Szleifer

2001

Biophysical Journal

154

169

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The thermodynamics and kinetics of protein adsorption are studied using a molecular theoretical approach. The cases studied include competitive adsorption from mixtures and the effect of conformational changes upon adsorption. The kinetic theory is based on a generalized diffusion equation in which the driving force for motion is the gradient of chemical potentials of the proteins. The time-dependent chemical potentials, as well as the equilibrium behavior of the system, are obtained using a molecular mean-field theory. The theory provides, within the same theoretical formulation, the diffusion and the kinetic (activated) controlled regimes. By separation of ideal and nonideal contributions to the chemical potential, the equation of motion shows a purely diffusive part and the motion of the particles in the potential of mean force resulting from the intermolecular interactions. The theory enables the calculation of the time-dependent surface coverage of proteins, the dynamic surface tension, and the structure of the adsorbed layer in contact with the approaching proteins. For the case of competitive adsorption from a solution containing a mixture of large and small proteins, a variety of different adsorption patterns are observed depending upon the bulk composition, the strength of the interaction between the particles, and the surface and size of the proteins. It is found that the experimentally observed Vroman sequence is predicted in the case that the bulk solution is at a composition with an excess of the small protein, and that the interaction between the large protein and the surface is much larger than that of the smaller protein. The effect of surface conformational changes of the adsorbed proteins in the time-dependent adsorption is studied in detail. The theory predicts regimes of constant density and dynamic surface tension that are long lived but are only intermediates before the final approach to equilibrium. The implications of the findings to the interpretation of experimental observations is discussed.

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Section: Introductionmentioning

confidence: 99%

Kinetics and Thermodynamics of Protein Adsorption: A Generalized Molecular Theoretical Approach

Fang

Szleifer

2001

Biophysical Journal

154

169

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“…Comparative assessment of the character of sorptive behaviour of materials produced from copolymers of various formulations, the level of values of S and the degree of intensity of the above regularities makes it possible to assume that characteristics of behaviour of the systems under consideration in protein sorption processes are determined not only by the presence of ionic groups but also by the fact that these groups are incorporated into polymer macromolecules that are capable of intensive hydrophobic interactions. High activity of aromatic polyamides in protein sorption processes was noted, for example, by the authors of reference [34] who conducted comparative investigations of sorptive and desorptive abilities of commercial membranes produced on the basis of various polymers. The results of investigations reported in the present paper indicate that in addition to coulomb forces hydrophobic interactions should be taken into account when predicting sorptive activity of materials under consideration.…”

Section: Resultsmentioning

confidence: 98%

Sorptive and Separation Properties of Ultrafiltration Membranes on the Basis of Sulfonate-Containing Polyamide with Respect to Bovine Serum Albumin

2012

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<p>Investigation of sorption of bovine serum albumin in the static mode and in ultrafiltration conditions by membranes produced from statistic copolymers of aromatic polyamides synthesized by polycondensation of the sodium salt of 4, 4/-diaminodiphenylamine-2-sulfo-acid and m-phenylenediamine in various ratios with chloroanhydride of isophthalic acid has been carried out. Interconnection has been established between the charge of protein macromolecules, concentration of fragments containing ionic groups in the aromatic polyamide and sorptive, separation and transport characteristics of membranes on its basis. It has been shown that dominant forces that determine membrane/protein interaction in the systems under consideration are coulomb forces, but the contribution of hydrophobic interactions is also significant. The results of mathematical processing of experimental data indicate that there is a good compliance of sorption isotherms with Langmuir’s model. Depending on the concentration of fragments containing ionic groups in the polyamide and pH of the solution, the calculated values of maximum sorption in sorbent/sorbate systems under consideration vary in the range of 0.028 to 0.338 mg/cm<sup>2</sup>. Dynamic investigations have shown that selectivity of the membranes is 85 to 98%. To assess the sorptive activity of the membranes in the course of ultrafiltration, indicators of sorption and sorptive losses calculated on the basis of the ratio of the change of mass content of protein in the process of filtration to the initial value have been used. Depending on the material used to produce the membrane and pH of the solution being filtered, sorptive losses range from 5 to 33%. Their minimum value is observed when pH is higher than the isoelectric point of the protein, i.e. in the field where protein macromolecules and the surface of the membrane have like charges.</p>

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“…In general, the intrinsic properties of BSA molecules, such as steric hindrance, electrostatic forces, and hydrophobic effects, reduce the wetting of the adsorbed layer [65]. This typical property of BSA makes it an efficient reagent to block nonspecific binding in immunoassay detection techniques [54,66].…”

Section: Discussionmentioning

confidence: 99%

Modification of polystyrene surface in aqueous solutions

Mielczarski

Jeyachandran

Mielczarski

et al. 2011

Journal of Colloid and Interface Science

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Diffusion model of protein adsorption and effect of protein layer composition on water permeability for ultrafiltration membranes

Cited by 7 publications

References 15 publications

Kinetics and Thermodynamics of Protein Adsorption: A Generalized Molecular Theoretical Approach

Kinetics and Thermodynamics of Protein Adsorption: A Generalized Molecular Theoretical Approach

Sorptive and Separation Properties of Ultrafiltration Membranes on the Basis of Sulfonate-Containing Polyamide with Respect to Bovine Serum Albumin

Modification of polystyrene surface in aqueous solutions

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