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ePT--the Electronic Newsletter of Pharmaceutical Technology
Michigan State University researchers have discovered a technique for viewing whole cells to gain an understanding of protein inclusion bodies.
East Lansing, MI (Dec. 10)-Michigan State University (MSU) researchers discovered a technique for viewing whole cells to gain an understanding of protein inclusion bodies. Several protein-based drugs are created by growing the protein within genetically modified Escherichia coli cells. One challenge, however, is that this process tends to generate insoluble aggregates known as inclusion bodies that trap folded proteins and are difficult to separate. Proteins within inclusion bodies, therefore, cannot be used. To recover the protein, scientists must break it down and refold it, which may delay development.
Using solid-state nuclear magnetic resonance (NMR) spectroscopy, the MSU team, led by chemistry professor David Weliky, can study the molecular structure of a single protein in whole cells. This analysis may yield clues as to how the inclusion body is formed. With this information, scientists may be able to extract the protein without unfolding it, thus speeding up manufacture and increasing efficiency. The traditional analytical method involved infrared spectroscopy using dehydrated samples.
“This study highlights our ability to probe the molecular structure of a single protein in whole cells and to apply advanced analytical and biochemical methods to a problem of general significance in biotechnology,” said Weliky in a prepared statement.