"Times are changing… We are changing them."
I graduated with a Ph.D. in Chemistry from the University of Oregon. I worked two years at a large defense firm as a “rocket scientist”, working on fiber optic gyroscopes and other things I still can’t talk about. I then worked two years at a small start-up formulating insulin for intra-nasal delivery. Then I came to Genentech in 1991 as a scientist in Pharmaceutical Research and Development (Pharm R&D). This is the group that figures out the best pH and excipients that make our proteins (our drugs) suitable enough to withstand manufacturing, storage, shipping, compounding, and whatever other conditions to which it may be exposed before it is administered to the patient. This requires a significant understanding of biochemistry and biophysics.
I became Director of Pharm R&D in 2001 and led the group until I stepped down from directorship in 2006 to get back in the lab. I never looked back.
I run the postdoc program in PTDU. Being the Post Doc coordinator is great! I get to learn from all these really smart and focused postdocs. They have really good ideas and while at Genentech, lots of resources… like a kid in a candy store… In the PTD postdoc program, postdocs interact and learn from other postdoc in other departments spanning Cell Culture, Purification, Analytical Chemistry, Drug Delivery, Formulation, and Biophysics. It’s hard to keep up with it all!
MAbs. 2013 Mar-Apr;5(2):306-22. Epub 2013 Feb 8.
Since stepping down as director my research has taken many directions. I study what happens in the frozen state (at -25C) of our monoclonal antibody (MAb) solutions. Freezing introduces dehydration, increased concentration, along with assorted insolubility of excipients and pH changes. We cannot store our MAb’s at -70C because of the multiple thousands of liters that we store at one time and thus the “higher” frozen temperatures allow for some mobility and thus potential instabilities.
I am also investigating the use of in silica molecular dynamics to predict chemical and physical stability of our monoclonal antibodies. These studies have crossed over into protein/protein interactions, thermal and pH stability of MAbs, and domain/domain interactions of full length MAbs that may be of biological significance. These are exciting times given that the computational speed and memory are now sufficient to study such large systems on a time frame that’s less than geological.