Topp: Difference between revisions
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<font size="+2">W</font>elcome! | <font size="+2">W</font>elcome! | ||
<p align="left"> | <p align="left"> In Dr. Elizabeth Topp's lab, we study protein formulation and stability. Protein drugs are one of the fastest growing sectors of the biopharmaceutical industry, offering new treatments for difficult diseases. Proteins are fragile, though, and can degrade during manufacturing and storage. Degradation reduces drug potency and can increase the potential for serious side effects. Our goal is to develop rational methods to formulate protein drugs based on a mechanistic understanding of the degradation processes that can occur. We're particularly interested in amorphous solids. More than 40% of current protein drugs are solids, yet little is known about the factors that control reactions in the amorphous state. </p> | ||
Click the links above to learn more about our research, our group members and our recent activities. Thanks for visiting! | Click the links above to learn more about our research, our group members and our recent activities. Thanks for visiting! | ||
[http://www.ipph.purdue.edu/news/fachighlights_Topp.php Topp Lab News] | |||
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Latest revision as of 08:51, 9 April 2015
Welcome!
In Dr. Elizabeth Topp's lab, we study protein formulation and stability. Protein drugs are one of the fastest growing sectors of the biopharmaceutical industry, offering new treatments for difficult diseases. Proteins are fragile, though, and can degrade during manufacturing and storage. Degradation reduces drug potency and can increase the potential for serious side effects. Our goal is to develop rational methods to formulate protein drugs based on a mechanistic understanding of the degradation processes that can occur. We're particularly interested in amorphous solids. More than 40% of current protein drugs are solids, yet little is known about the factors that control reactions in the amorphous state.
Click the links above to learn more about our research, our group members and our recent activities. Thanks for visiting!
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