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Preparation of Poly(pentafluorophenyl acrylate) Functionalized SiO2 Beads for Protein Purification

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Protein purification with polymeric affinity membranes containing functionalized poly(acid) brushes.

Parul Jain¹, Mukesh Kumar Vyas, James H Geiger

¹Department of Chemistry Michigan State University East Lansing, Michigan 48824, USA.

Biomacromolecules

|March 2, 2010

Summary

Modified nylon membranes offer rapid, high-capacity protein purification. Functionalized poly(2-(methacryloyloxy)ethyl succinate) (poly(MES)) brushes enable efficient ion-exchange and affinity-based separation of target proteins from complex mixtures.

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Area of Science:

Biomaterials Science
Protein Chemistry
Separation Science

Background:

Porous membranes are crucial for bioseparations.
Existing methods for protein purification can be time-consuming and costly.
Developing novel materials for efficient protein purification is essential.

Purpose of the Study:

To develop and characterize porous nylon membranes modified with poly(acid) brushes for protein purification.
To evaluate the ion-exchange and metal-ion affinity capabilities of these modified membranes.
To demonstrate the rapid isolation of His-tagged proteins from cell extracts.

Main Methods:

Modification of porous nylon membranes with poly(2-(methacryloyloxy)ethyl succinate) (poly(MES)) brushes.
Functionalization of poly(MES) brushes with nitrilotriacetate (NTA)-Ni(2+) complexes.
Binding capacity studies using lysozyme and His-tagged ubiquitin.
Rapid isolation of His-tagged cellular retinaldehyde-binding protein from cell extracts.

Main Results:

Poly(MES) brush-modified membranes exhibited high lysozyme binding capacity (118 +/- 8 mg/cm(3)).
Poly(MES)-NTA-Ni(2+) functionalized membranes showed high His-tagged ubiquitin binding capacity (85 +/- 2 mg/cm(3)).
Rapid (<10 min) isolation of His-tagged protein from cell extracts with purity comparable to commercial columns was achieved.

Conclusions:

Functionalized poly(MES) brushes on porous nylon membranes provide an effective platform for rapid protein purification.
These membranes offer high binding capacities for both general ion-exchange and specific affinity interactions.
The developed membranes are promising for efficient and fast purification of His-tagged proteins from complex biological samples.