Journal
SEPARATION SCIENCE AND TECHNOLOGY
Volume 52, Issue 2, Pages 276-286Publisher
TAYLOR & FRANCIS INC
DOI: 10.1080/01496395.2016.1206934
Keywords
Arg-tag; ATRP; fusion protein; membrane chromatography; surface modification
Funding
- National Institutes of Health [1 R15 GM094676-01]
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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.
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