Modern drug development faces a problem in separating proteins from deadly impurities in the purification process.
Scientists within the Center for Biotechnology and Interdisciplinary Studies (CBIS) at Rensselaer Polytechnic Institute are using nuclear magnetic resonance (NMR) to understand and improve an important protein purification process.
"We hope to use our insights to help those in the industry develop improved processes to provide much less expensive drugs and dramatically reduce healthcare costs," said paper author and William Weightman Walker Professor of Polymer Engineering Steven Cramer of Rensselaer.
His team's findings are published in the Sept. 2 online early edition of the journal Proceedings of the National Academy of Sciences
(PNAS ) in a paper titled "Evaluation of protein absorption and preferred binding regions in multimodal chromatography using NMR." The research was funded by the National Science Foundation (NSF).
The process of multimodal chromatography has recently generated significant interest in the pharmaceutical industry. At its most basic, this process separates proteins from their surrounding materials, such as DNA and other proteins. The process works by encouraging the desired protein to stick to a material that contains a ligand, a type of molecular glue. Each ligand is only attracted to certain parts of certain proteins. Having been separated from the mixture, the specific protein can now be obtained in purer form, facilitating its eventual use as a biotherapeutic.