Affinity membrane adsorbers for binding arginine-rich proteins

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. Me...

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Bibliographic Details
Published in:Separation science and technology 2017-01, Vol.52 (2), p.276-286
Main Authors: Chenette, Heather C. S., Welsh, James M., Husson, Scott M.
Format: Article
Language:English
Subjects:
Affinity
Analytical methods
Arg-tag
Arginine
ATRP
Binding
Binding energy
Cancer
Capacity
Energy measurement
Financing
fusion protein
Infrared spectroscopy
Kinetics
Ligands
Lysozyme
membrane chromatography
Membranes
Peptides
Phosphonates
Polymers
Protein purification
Proteins
Selectivity
Separation
Spectroscopic analysis
Spectrum analysis
surface modification
Water purification
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Summary: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.
ISSN:0149-6395
1520-5754
DOI:10.1080/01496395.2016.1206934