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September 06, 2010
Polymer Conjugates: How to Purify Proteins Using Polymers
Chien-Wen Chang, Thi H. Nguyen, and Heather D. Maynard*
Proteins are important therapeutics and essential agents to study biological processes. Critical to these applications are efficient and inexpensive methods to purify these biomolecules. Heather Maynard and co-workers (UCLA) introduce a single-step method to "pull down" or isolate proteins that contain a common genetic tag, glutathione S-transferase (GST). Glutathione (GSH, a natural reductant found in living cells) reversibly interacts with GST via precise molecular recognition in aqueous solution. The researcher synthesized a pyridyl disulfide-poly(N-isopropylacrylamide) (pNIPAAm) that could be conjugated to GSH with high efficiency (95% in 30 minutes). GST was successfully thermoprecipitated upon heating the GSH–pNIPAAm above the lower critical solution temperature. Due to its simplicity and high efficiency, this method holds great potential for large-scale purification of GST-tagged proteins.
Macromol. Rapid Commun., DOI: 10.1002/marc.201000333
Other contributions to the article series on polymer conjugates can be found here.