Adsorption of polyethylene-glycolated bovine serum albumin on macroporous and polymer-grafted anion exchangers

Zhu, Mimi; Carta, Giorgio

doi:10.1016/j.chroma.2013.12.007

Cited by 26 publications

(30 citation statements)

References 30 publications

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“…A common approach is to determine q 0 from a potentiometric titration of the resin or by the frontal exchange of counterions and to determine K e and z from linear gradient elution (LGE) at low protein loads for conditions where the protein elutes in the linear range of the isotherm. For these conditions, the Na + concentration at which the protein elutes,

C_{{italicNa}^{+}}^{E}

is related to the normalized gradient slope by the following equation [23][24][25][26]:

γ = \frac{1}{ϕ} \int_{C_{{Na}^{+}}^{0}}^{C_{{Na}^{+}}^{E}} \frac{{italicdC}_{{Na}^{+}}}{A {true(C_{{italicNa}^{+}} false)}^{- z} + ε_{p} false(K_{D} - 1 false)}

where A = K e ( q 0 ) z . The normalized gradient slope is given by γ = ε Δ C Na + / CV G , where ε is the column void fraction, Δ C Na + the difference between final and initial Na + concentrations, CV G the duration of the gradient in column volume units, and ϕ = (1 − ε )/ ε is the phase ratio.…”

Section: Theoretical Developmentmentioning

confidence: 99%

Systematic interpolation method predicts protein chromatographic elution from batch isotherm data without a detailed mechanistic isotherm model

Creasy

Barker

Yan

et al. 2015

Biotechnology Journal

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A method is developed to predict protein chromatographic behavior from batch isotherm using a a systematic empirical interpolation (EI) scheme and without relying on a mechanistic description of the dependence of protein binding on protein and salt concentration. Coupled with a lumped kinetic model with rate parameters determined from HETP measurements for non-binding conditions, the EI scheme is used to numerically predict the column behavior. For two experimental cation exchange systems considered in this work, lysozyme on SP-Sepharose-FF and a monoclonal antibody on POROS XS, predictions based on the EI scheme are in excellent agreement with experimental elution profiles under highly overloaded conditions without using any adjustable parameters. A qualitative study of the sensitivity of predicting protein elution profiles to the precision, granularity, and extent of the batch adsorption data is conducted. Based on the results for a hypothetical system, whose properties are comparable to those found in practice for protein cation exchange chromatography the results of this show that the interpolation scheme is relatively insensitive, requiring only that the ranges of protein and salt concentrations in the experimental dataset overlap those under which the protein actually elutes from the column and along with a 10% measurement precision.

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C_{{italicNa}^{+}}^{E}

is related to the normalized gradient slope by the following equation [23][24][25][26]:

γ = \frac{1}{ϕ} \int_{C_{{Na}^{+}}^{0}}^{C_{{Na}^{+}}^{E}} \frac{{italicdC}_{{Na}^{+}}}{A {true(C_{{italicNa}^{+}} false)}^{- z} + ε_{p} false(K_{D} - 1 false)}

Section: Theoretical Developmentmentioning

confidence: 99%

Systematic interpolation method predicts protein chromatographic elution from batch isotherm data without a detailed mechanistic isotherm model

Creasy

Barker

Yan

et al. 2015

Biotechnology Journal

Self Cite

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show abstract

“…However, while the rate was essentially independent of the direction of transport for the macroporous resin, the rates observed for the polymer-grafted resin were different dependent on whether native and deamidated isoforms were adsorbed simultaneously or in a consecutive manner, with the native species displacing the deamidated isoforms. Tao et al [31], Perez et al [32], and Zhu and Carta [33] also used CLSM to study the evolution of intraparticle concentration profiles during adsorption of protein mixtures in CEX and AEX resins for, respectively, deamidated mAb mixtures, multiple mAbs, and mixtures of native and PEGylated proteins. These authors considered both macroporous and polymer-grafted resins.…”

Section: Introductionmentioning

confidence: 98%

Adsorption equilibrium and kinetics of monomer–dimer monoclonal antibody mixtures on a cation exchange resin

Reck

Pabst²,

Hunter³

et al. 2015

Journal of Chromatography A

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“…The four experimental resins used in this work were provided by Bio‐Rad Laboratories (Hercules, CA, USA) and are listed in Table along with some of their relevant properties. All four are based on similar polymeric spherical beads based on acrylamido and vinyl co‐monomers and are variants of the UNOsphere and Nuvia™ resins described in previous work . Particle diameters were determined by optical microscopy.…”

Section: Methodsmentioning

confidence: 99%

“…The binding capacity was found to be about three times greater and adsorption rates about two times higher for the polymer‐grafted resin vs the ungrafted base matrix. More recently, Zhu and Carta studied the adsorption behavior of BSA and PEGylated BSA on AEX resins with quaternary ammonium ion functionality on grafted and ungrafted UNOsphere‐type resins. Binding capacity and kinetics were higher for BSA on the polymer‐grafted resin but these advantages were diminished for PEGylated BSA.…”

Section: Introductionmentioning

confidence: 99%

Protein adsorption in anion exchange resins – effects of polymer grafting, support structure porosity, and protein size

Zhu

Fuks

Carta

2017

J of Chemical Tech & Biotech

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BACKGROUND: Anion exchange resins are used extensively for the purification of acidic proteins. Grafting charged polymers to a rigid porous structure has been shown to improve performance under varying conditions. Understanding the underlying mechanisms is important for the optimum design and selection of material properties and operating conditions. RESULTS: Positively charged grafted polymers incorporated into a rigid, porous polymeric backbone structure are found to significantly enhance adsorption capacity and kinetics of the proteins bovine serum albumin (BSA, M r ∼ 65 kDa) and thyroglobulin (Tg, M r ∼ 660 kDa) but under different conditions. For the smaller BSA, binding increases with grafted polymer length and content and decreases with salt concentration. For the much larger Tg, binding increases with the addition of some salt for the polymer-grafted resins but can be lower than that observed for ungrafted resins without added salt. This behavior is caused by diffusional hindrance due to the bound protein. Increasing the length of the grafted polymer or the pore size of the backbone improves the Tg adsorption kinetics. CONCLUSION: Protein adsorption is controlled by different mechanisms dependent on polymer grafting, backbone structure, and size of the adsorbed protein. Optimum selection of resin properties and conditions is needed to maximize adsorption capacity and mass transfer kinetics.

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Adsorption of polyethylene-glycolated bovine serum albumin on macroporous and polymer-grafted anion exchangers

Cited by 26 publications

References 30 publications

Systematic interpolation method predicts protein chromatographic elution from batch isotherm data without a detailed mechanistic isotherm model

Systematic interpolation method predicts protein chromatographic elution from batch isotherm data without a detailed mechanistic isotherm model

Adsorption equilibrium and kinetics of monomer–dimer monoclonal antibody mixtures on a cation exchange resin

Protein adsorption in anion exchange resins – effects of polymer grafting, support structure porosity, and protein size

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