New way of viewing cells could lead to easier routes for drug manufacture

Dec 10, 2008

Research by a Michigan State University chemist could eventually lead to a quicker and easier way of developing protein-based drugs that are key to treating a number of diseases, including cancer, diabetes and hepatitis.

Proteins used in drug manufacture and research often are made within genetically modified Escherichia coli, a one-cell bacteria. That protein tends to collect into what scientists call inclusion bodies. Those hard-to-separate clumps render up to 95 percent of the protein unusable, according to associate chemistry professor David P. Weliky.

Some can be recovered by breaking down the protein to separate it, but because protein structure determines its function, another step must be added to "refold" it into its original configuration.

Weliky and colleagues took a closer look at the structure of the proteins that make up these inclusion bodies. Learning what makes them stick together might yield some clues as to how to separate them, he said, and that could make the manufacturing process more efficient.

Instead of employing more commonly used infrared spectroscopy to look at dehydrated samples, the researchers used nuclear magnetic resonance spectroscopy using whole cells. That technology analyzes the magnetic properties of an atom's nucleus.

While best known as medical diagnostic imaging technology, Weliky and colleagues view NMR as a powerful approach to analyzing biological molecules, including bacterial inclusion bodies. Because the inclusion body protein appeared to be predominantly folded rather than unfolded, it might be possible to extract protein without separating and then refolding, Weliky said.

"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," Weliky said.

Source: Michigan State University

Explore further: Scientists find clues to cancer drug failure

add to favorites email to friend print save as pdf

Related Stories

Study uncovers secrets of a clump-dissolving protein

Jan 22, 2015

Workhorse molecules called heat-shock proteins contribute to refolding proteins that were once misfolded and clumped, causing such disorders as Parkinson's disease, amyotrophic lateral sclerosis, and Alzheimer's ...

A tighter fit with artificial DNA

Jul 19, 2013

An artificial base that enhances the protein-binding affinity and selectivity of DNA expands the DNA machinery.DNA aptamers are expected to play an important role in the diagnosis and treatment of various ...

How cells get a skeleton

Jun 10, 2013

The mechanism responsible for generating part of the skeletal support for the membrane in animal cells is not yet clearly understood. Now, Jean-François Joanny from the Physico Chemistry Curie Unit at the Curie Institute ...

Engineers' nanoantennas improve infrared sensing

May 20, 2013

(Phys.org) —A team of University of Pennsylvania engineers has used a pattern of nanoantennas to develop a new way of turning infrared light into mechanical action, opening the door to more sensitive infrared ...

Recommended for you

Scientists find clues to cancer drug failure

4 hours ago

Cancer patients fear the possibility that one day their cells might start rendering many different chemotherapy regimens ineffective. This phenomenon, called multidrug resistance, leads to tumors that defy ...

Smart crystallization

9 hours ago

A novel nucleating agent that builds on the concept of molecularly imprinted polymers (MIPs) could allow crystallographers access to proteins and other biological macromolecules that are usually reluctant ...

Supersonic electrons could produce future solar fuel

10 hours ago

Researchers from institutions including Lund University have taken a step closer to producing solar fuel using artificial photosynthesis. In a new study, they have successfully tracked the electrons' rapid transit through ...

User comments : 0

Please sign in to add a comment. Registration is free, and takes less than a minute. Read more

Click here to reset your password.
Sign in to get notified via email when new comments are made.