Nonspecific Effects of Ion Exchange and Hydrophobic Interaction Adsorption Processes

Korfhagen, Joseph J.; Dias-Cabral, A.C.; Thrash, Marvin E.

doi:10.1080/01496391003793876

Cited by 18 publications

(14 citation statements)

References 32 publications

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“…The profile changes are probably related to the increased presence of the boronate anion in the ligand structure (mainly due to the shift in the acid–base equilibrium caused by the increase in the pH), which is able to promote electrostatic interactions with the anti‐IL8 mAb (Figure A). For this type of interactions to occur, water and ions have to be released from the surface of the adsorbent and protein, which leads to a consumption of energy and to an increase of entropy . At pH 9.0, the ligand will be predominantly present in its tetrahedral forms — the ones obtained by hydroxylation of the boronic acid or by B–F coordination (Figure A,B, respectively).…”

Section: Resultsmentioning

confidence: 99%

Mobile‐Phase Modulators as Salt Tolerance Enhancers in Phenylboronate Chromatography: Thermodynamic Evaluation of the Mechanisms Underlying the Adsorption of Monoclonal Antibodies

Rosa

Wagner

Silva

et al. 2019

Biotechnology Journal

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Phenylboronate chromatography has been employed for bioseparation applications though details concerning the mechanisms of interaction between the ligand and macromolecules remain widely unknown. Here, the phenomena underlying the adsorption of an anti-human interleukin-8 (anti-IL8) monoclonal antibody (mAb) onto an m-aminophenylboronic acid (m-APBA) ligand in the presence of different mobile-phase modulators (NaF/MgCl 2 /(NH 4 ) 2 SO 4 ) and under different pH values (7.5/8.5/9.0) is investigated. Flow microcalorimetry (FMC) is applied to measure instantaneous heat energy transfer, providing insights about the role of specific and nonspecific interactions involved in the adsorptive process. Results show that the adsorption of anti-IL8 mAb to m-APBA is enthalpically driven, corroborating the presence of the reversible esterification reaction between boronic acid or boronates and cis-diol-containing molecules. Nevertheless, for all mobile-phase modulators studied, changes in thermogram profiles are observed as well as reductions in the net heat of adsorption when increasing the pH. Overall, FMC and parallel chromatographic experiments data suggest that ligand salt tolerance could be enhanced using mobile-phase modulators, with all salts studied promoting the specific cis-diol interactions and reducing nonspecific interactions. The last feature is more noticeable at pH values above ligand's pK a , mainly due to the ability of NaF and (NH 4 ) 2 SO 4 to diminish electrostatic interactions when compared to the commonly used NaCl.

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Section: Resultsmentioning

confidence: 99%

Mobile‐Phase Modulators as Salt Tolerance Enhancers in Phenylboronate Chromatography: Thermodynamic Evaluation of the Mechanisms Underlying the Adsorption of Monoclonal Antibodies

Rosa

Wagner

Silva

et al. 2019

Biotechnology Journal

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“…Thermograms for GlyGly adsorption on prepared xerogels were collected at room temperature using flow microcalorimetry (Microscal FMC 4 Vi, Microscal Limited, London, UK) following previously reported methods [9,11,12]. The material was packed into a bed in the FMC and equilibrated overnight with flowing mobile phase (0.01 mol L −1 borax solution/EtOH (1:1, v/v)).…”

Section: Flow Sorption Microcalorimetry (Fmc)mentioning

confidence: 99%

“…Both procedures were optimized and the imprinting effect of the molecularly imprinted silica particles was evaluated by solid phase extraction (SPE). Additionally, flow microcalorimetry (FMC) has for the first time been used here in order to study the interactions of the prepared xerogels with the target, allowing an improved understanding of the driving forces and mechanisms involved in the interaction [9][10][11][12].…”

Section: Introductionmentioning

confidence: 99%

Synthesis of glycylglycine-imprinted silica microspheres through different water-in-oil emulsion techniques

Ornelas

Loureiro

Araújo

et al. 2013

Journal of Chromatography A

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“…For a concave curse of the adsorption isotherm, which is often reported for proteins on hydrophobic surfaces [36], the BET isotherm can be used. The BET equation for liquid-solid adsorption equilibrium can be expressed as follows [37,38]:…”

Section: Steady State Mass Transport In the Cp Layermentioning

confidence: 99%

“…For a concave curse of the adsorption isotherm, which is often reported for proteins on hydrophobic surfaces , the BET isotherm can be used. The BET equation for liquid–solid adsorption equilibrium can be expressed as follows :

q^{*} = \frac{q^{\infty} K_{normalS} C_{δ}}{(1 - K_{normalL} C_{δ}) (1 - K_{L} C_{δ} + K_{normalS} C_{δ})}

where K S and K L are the equilibrium constants characterizing interactions between the adsorbent surface and the protein and between the adsorbed molecules of proteins in adjacent layers, respectively.…”

Section: Introductionmentioning

confidence: 99%

A shortcut method for evaluation of protein deposition onto the membrane surface in crossflow ultrafiltration

Muca

Pia̧tkowski

Antos

2016

Engineering in Life Sciences

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In this study, a procedure for quantifying the surface deposition of proteins in crossflow ultrafiltration has been developed. The procedure consists of determining the protein adsorption behavior onto the membrane surface from a few dynamic measurements performed in a nonfiltration and a filtration mode, and evaluating the concentration polarization (CP) layer thickness based on the adsorption data. To predict the interdependence between the protein adsorption and CP, a simplified mathematical model has been formulated. The model was used to assess the protein adsorption and thus yield reduction in the ultrafiltration process at different protein concentration in the solution. As a case study, ultrafiltration of aqueous solutions of BSA and lysozyme (LYZ) was examined on a polyethersulfone membrane with the molecular weight cutoff of 10 or 100 kDa. The protein concentration in the solutions varied within a relatively low concentration range, i.e. below 10 mg mL−1, characteristic for solvent exchange between sequential operations of protein purification by chromatography and extraction. Both proteins markedly differed in the mechanism of surface deposition; for BSA hydrophobic interactions were suggested to be dominant, whereas in case of LYZ electrostatic interactions contributed the most to the deposition mechanism. The effect of additives of the protein solutions, i.e. inorganic salts, PEG, and urea depended on the adsorption mechanism and was also specific for each protein. Nevertheless, the proposed procedure performed well in the evaluation of surface deposition and yield reduction, regardless of the protein type and its solvent environment.

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Nonspecific Effects of Ion Exchange and Hydrophobic Interaction Adsorption Processes

Cited by 18 publications

References 32 publications

Mobile‐Phase Modulators as Salt Tolerance Enhancers in Phenylboronate Chromatography: Thermodynamic Evaluation of the Mechanisms Underlying the Adsorption of Monoclonal Antibodies

Mobile‐Phase Modulators as Salt Tolerance Enhancers in Phenylboronate Chromatography: Thermodynamic Evaluation of the Mechanisms Underlying the Adsorption of Monoclonal Antibodies

Synthesis of glycylglycine-imprinted silica microspheres through different water-in-oil emulsion techniques

A shortcut method for evaluation of protein deposition onto the membrane surface in crossflow ultrafiltration

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