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Related Concept Videos

Affinity Chromatography01:03

Affinity Chromatography

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Affinity chromatography is a powerful technique extensively utilized for separating and purifying specific biomolecules from complex mixtures. It capitalizes on the highly selective binding between an analyte and its counterpart, such as antibody-antigen interactions. The counterpart is immobilized on the stationary phase, forming an affinity column. The stationary phase typically consists of solid support, such as agarose or porous glass beads, immobilizing the affinity ligand. The mobile...
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Immunoprecipitation, or IP, is a widely used technique that employs protein-antibody interactions to isolate proteins or protein complexes in their native state for studying protein-protein interactions, quaternary structures, or supramolecular complexes. Various modifications of the technique, including chromatin IP, cross-linking IP, and fluorescence IP, are commonly used.
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Proteins are involved in several cellular processes and biochemical reactions. Analyzing a specific protein of interest requires it to be isolated from the other proteins in the cell. This is achieved by overexpressing the specific gene in a suitable host to produce large quantities of the target protein. A tag or label is recombined with the gene to produce a fusion protein containing the target protein and the tag. The tags on these fusion proteins can then be used for easy detection and...
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Resolving Affinity Purified Protein Complexes by Blue Native PAGE and Protein Correlation Profiling
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Affinity-Based Purification of Polyisocyanopeptide Bioconjugates.

Roel Hammink1,2, Loek J Eggermont2, Themistoklis Zisis1

  • 1Department of Molecular Materials, Institute for Molecules and Materials, Radboud University , Heyendaalseweg 135, 6525 AJ Nijmegen, The Netherlands.

Bioconjugate Chemistry
|August 29, 2017
PubMed
Summary

Researchers developed a new affinity purification method for synthetic polymers called polyisocyanopeptides (PICs). This method efficiently purifies PIC-biomolecule conjugates, enabling advanced biomedical applications.

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Synthesis of Protein Bioconjugates via Cysteine-maleimide Chemistry
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Area of Science:

  • Biomaterials Science
  • Polymer Chemistry
  • Nanotechnology

Background:

  • Water-soluble polyisocyanopeptides (PICs) are synthetic polymers mimicking natural protein filaments.
  • PICs possess unique semiflexible properties and nanometer-scale lengths, enabling biomedical applications like tissue engineering and cancer immunotherapy.
  • Efficient synthesis and purification of PIC-biomolecule conjugates are crucial for advancing PIC applications.

Purpose of the Study:

  • To develop an efficient and controlled method for purifying polyisocyanopeptide (PIC)-biomolecule conjugates.
  • To overcome limitations of standard purification techniques for large, semiflexible polymers.
  • To enable high-purity bioconjugates for direct application in biomedical fields.

Main Methods:

  • Developed an affinity-based purification strategy using biotin as an affinity tag.
  • Synthesized biotinylated PICs (biotinPICs) with controlled biotin density.
  • Utilized monoavidin resin for binding and elution of biotinPICs in aqueous solution.

Main Results:

  • Successfully synthesized and purified two types of biotinPIC-protein conjugates: one with alkaline phosphatase (PhoA) and another with anti-CD3 antibodies.
  • Achieved high purity (>90%) for the bioconjugates without compromising protein activity.
  • Demonstrated simplified analysis and direct application of the purified bioconjugates.

Conclusions:

  • Introduced a novel, effective affinity-based purification method for polyisocyanopeptide (PIC)-biomolecule conjugates.
  • The method enables high-purity bioconjugates, facilitating their use in advanced biomedical applications.
  • This technique holds potential for purifying other challenging bioconjugates.