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Ion exchange chromatography separates charged molecules from a solution by reversibly exchanging them with mobile, or 'active', ions associated with the oppositely charged stationary phase. This method can be used to separate ions, soften and deionize water, and purify solutions. The polymers comprising the ion-exchange column are high-molecular-weight and chemically stable polymers, crosslinked to be porous and essentially insoluble. They are also functionalized with either acidic or...
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Ion-exchange chromatography, or IEC, is a technique for separating ions based on their affinity for the stationary phase. The stationary phase is a cross-linked polymer resin with covalently attached ionic functional groups. The functional groups can be either positively charged (cation exchangers) or negatively charged (anion exchangers). A cation exchanger consists of a polymeric anion and active cations, while an anion exchanger is a polymeric cation with active anions. The choice of...
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In certain chromatographic separations, solutes transfer between the mobile phase and the stationary phase via sorption, which typically refers to the process of adsorption. For many chromatographic systems, the sorption process often depends on the polarity of the compounds—an expression of the overall dipole moment within the molecule. During the separation process, there is competition between the solute and solvent for adsorption to the stationary phase. Highly polar compounds and...
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Complexation Equilibria: The Chelate Effect01:19

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In complexation reactions, metal atoms or cations interact with ligands to form donor-acceptor adducts called metal complexes. Ligands that bind through one donor site are monodentate, ligands with two donor sites are bidentate, and those with more than two donor sites are polydentate ligands. For example, ethylene diamine is a bidentate ligand that binds through two nitrogen donor atoms, forming a five-membered ring. EDTA is a polydentate ligand that binds through four oxygen and two nitrogen...
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Metal ions can be separated from one another by complexation with organic ligands–the chelating agent– to form uncharged chelates. Here, the chelating agent must contain hydrophobic groups and behave as a weak acid, losing a proton to bind with the metal. Since most organic ligands used in this process are insoluble or undergo oxidation in the aqueous phase, the chelating agent is initially added to the organic phase and extracted into the aqueous phase. The metal-ligand complex is...
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Polydentate ligands are most widely used in complexometric titrations because they form more stable complexes with the metal ions than mono- or bidentate ligands due to the chelate effect. Examples of polydentate ligands are ethylenediaminetetraacetic acid (EDTA), crown ethers, and cryptands. The most important feature of optimal polydentate ligands is the ability to form 1:1 complexes in a single-step process. Amino carboxylic acid derivatives are frequently used as complexing agents. EDTA is...
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Protein adsorption in polyelectrolyte brush type cation-exchangers.

Rushd Khalaf1, Bertrand Coquebert de Neuville1, Massimo Morbidelli1

  • 1Institute for Chemical and Bioengineering, ETH Zurich, 8093 Zurich, Switzerland.

Journal of Chromatography. A
|October 23, 2016
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Summary

Polyelectrolyte brush (PEB) ion exchangers exhibit unique protein adsorption behaviors, shifting from anti-Langmuirian to Langmuirian interactions with increased injection volumes. This is due to proteins utilizing the 3D structure of PEB materials during purification.

Keywords:
3D adsorptionAnti-Langmuir to Langmuir behaviorIon-exchange chromatographyMulti-layer adsorptionPolyelectrolyte brushes

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Area of Science:

  • Biochemistry
  • Materials Science
  • Chromatography

Background:

  • Ion exchange chromatography materials functionalized with polyelectrolyte brushes (PEB) are increasingly used in protein purification.
  • Protein adsorption on PEB materials differs from traditional materials due to 3D partitioning within the brushes.
  • Existing studies often apply traditional chromatography methods to analyze PEB behavior, potentially overlooking unique interactions.

Purpose of the Study:

  • To investigate and explain the unconventional chromatographic behavior of proteins on polyelectrolyte brush ion exchangers.
  • To elucidate the relationship between protein adsorption, injection volume, and the 3D structure of PEB materials.
  • To develop an experimental and model-based description for PEB chromatography.

Main Methods:

  • Utilized ion exchange chromatography with polyelectrolyte brush functionalized materials.
  • Performed experiments with varying protein injection volumes to observe chromatographic peak shapes.
  • Developed and applied a model-based approach to describe the observed adsorption phenomena.
  • Analyzed the adsorption behavior of several different proteins.

Main Results:

  • Observed unconventional chromatographic behavior, including anti-Langmuirian and Langmuirian peak shapes, correlating with increasing injection volumes.
  • Demonstrated that proteins fully utilizing the 3D PEB structure exhibit this unique behavior.
  • Showed that proteins not fully utilizing the 3D structure display traditional ion exchange behavior.
  • Provided an experimental and model-based explanation for the observed phenomena.

Conclusions:

  • The 3D partitioning of proteins into polyelectrolyte brushes is the primary cause of unconventional chromatographic behavior.
  • Protein adsorption dynamics on PEB materials are dependent on the extent to which proteins engage with the brush's 3D architecture.
  • Understanding this 3D partitioning is crucial for optimizing protein purification using PEB ion exchangers.