ArticleSeparation science and technology2017
Affinity membrane adsorbers for binding arginine-rich proteins.
Article in Separation science and technology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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Who cites it
2 citing papers in PubMed, 5 citations in OpenAlex.
- Molecularly Imprinted Affinity Membrane: A Review.ACS omega · 2022Review
- Recent Developments of Liquid Chromatography Stationary Phases for Compound Separation: From Proteins to Small Organic Compounds.Molecules (Basel, Switzerland) · 2022Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
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 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.
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Registered trials
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