Exploring science is typically characterized by a lot of puzzles, frustrations or even failures. This weblog is mainly intended to record my working, thinking and knowledge acquisitions. I expect that some reflection would refresh my mind from time to time, and motivate me to move further, and hopefully give me a better view about even changing the landscape of bioinformatics.
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Thursday, February 24, 2011
Research scientists develop powerful new methodology for stabilizing proteins
A team of scientists at The Scripps Research Institute has discovered a new way to stabilize proteins - the workhorse biological macromolecules found in all organisms. Proteins serve as the functional basis of many types of biologic drugs used to treat everything from arthritis, anemia, and diabetes to cancer.
As described in the February 4, 2011 edition of the journal Science, when the team attached a specific oligomeric array of sugars called a "glycan" to proteins having a defined structure, the proteins were up to 200 times more stable in the test tube. In the body, this stability may translate into longer half-lives for therapies, possibly lowering the overall cost of treatment for certain protein-based drugs and requiring patients to have fewer injections during a course of treatment.
The work may have major implications for the drug industry because there are a large number of protein-based drugs on the market, more in clinical trials, and many more under development worldwide. Nearly all of these protein-based drugs have glycans attached to them and are therefore called "glycoproteins". Glycoprotein-based drugs can be quite expensive to produce and usually need to be administered intravenously.
One of the challenges in producing these drugs has been increasing their stability, which generally extends their half-life in the bloodstream - issues that the new discovery appears to address directly.
"We've now provided engineering guidelines for glycoprotein stability," said Scripps Research Professor Jeffery W. Kelly, who is chair of the Department of Molecular and Experimental Medicine, Lita Annenberg Hazen Professor of Chemistry, and member of The Skaggs Institute for Chemical Biology at Scripps Research. Kelly led the study with Scripps Research Associate Professor Evan Powers and Staff Scientist Sarah R. Hanson, in collaboration with Research Associates Elizabeth K. Culyba, Joshua Price, and colleagues.