Work

Affinity membrane adsorbers for binding arginine-rich proteins

Year: 2016

Type: article

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.

Source: Separation Science and Technology

DOI: 10.1080/01496395.2016.1206934

Authors: Heather C. S. Chenette, James M. Welsh, Scott M. Husson

Institution: Clemson University

Language: English

Topic: Protein purification and stability

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

SDG: Good health and well-being

Open Access status: green

Funders: Clemson University, National Institutes of Health, National Institute of General Medical Sciences, Division of Materials Research