Affinity membrane adsorbers for binding arginine-rich proteins
| Autor: | James M. Welsh, Scott M. Husson, Heather C. S. Chenette |
|---|---|
| Rok vydání: | 2016 |
| Předmět: |
chemistry.chemical_classification
Chromatography Arginine Chemistry Process Chemistry and Technology General Chemical Engineering Infrared spectroscopy Filtration and Separation Peptide 02 engineering and technology General Chemistry 010402 general chemistry 021001 nanoscience & nanotechnology 01 natural sciences Fusion protein Combinatorial chemistry Phosphonate Receptor–ligand kinetics 0104 chemical sciences chemistry.chemical_compound Membrane Lysozyme 0210 nano-technology |
| DOI: | 10.6084/m9.figshare.3469826.v1 |
| Popis: | Delivering protein chemotherapeutics into cancer cells is a challenge. Fusing the protein to an arginine-rich cell-penetrating peptide offers a possible solution. The goal of this work was to develop an affinity membrane for the purification of Arg-rich fusion proteins via capture chromatography. Membranes were prepared by grafting polymers bearing diethyl-4-aminobenzyl phosphonate (D4ABP) ligands from macroporous membrane supports. Incorporation of D4ABP was studied by infrared spectroscopy and energy dispersive spectroscopy. Protein-binding capacities of 3 mg lysozyme/mL were measured. While further studies are required to evaluate binding kinetics and Arg-selectivity, achieving higher protein-binding capacity is needed before investment in such studies. |
| Databáze: | OpenAIRE |
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