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Professors John F. Carpenter and Theodore W. Randolph: 2 Giants With a Special Synergy in the Field of Biopharmaceutical Science and Engineering

Published:October 29, 2019DOI:https://doi.org/10.1016/j.xphs.2019.10.049
      The story of how Professors John Carpenter and Ted Randolph joined forces to revolutionize biopharmaceutical chemistry begins over 3 decades ago. They both independently made their marks in the field of protein chemistry by the late 1980s; John, with his landmark work revealing the mechanism of protein stability by cosolutes in the frozen and freeze-dried states,
      • Carpenter J.F.
      • Crowe J.H.
      The mechanism of cryoprotection of proteins by solutes.
      ,
      • Carpenter J.F.
      • Crowe J.H.
      Modes of stabilization of a protein by organic solutes during desiccation.
      and Ted, with his pioneering work developing stable enzyme reaction conditions in supercritical carbon dioxide.
      • Randolph T.W.
      • Clark D.S.
      • Blanch H.W.
      • Prausnitz J.M.
      Enzymatic oxidation of cholesterol aggregates in supercritical carbon dioxide.
      ,
      • Randolph T.W.
      • Clark D.S.
      • Blanch H.W.
      • Prausnitz J.M.
      Cholesterol aggregation and interaction with cholesterol oxidase in supercritical carbon dioxide.
      Then, in the early 1990s, they both fortuitously landed at the University of Colorado: Ted in the Department of Chemical Engineering in Boulder, and John at the Department of Pharmaceutical Sciences in Denver. At the beginning of their academic careers, they were introduced through mutual friend and collaborator, Dr. Jeffrey L. Cleland, and starting in the mid-1990s began a collective wave of research in protein physical chemistry. This research transformed protein drug product and formulation development from an empirical, brute-force approach to an efficient, rational approach rooted in fundamental protein physical stability mechanisms.

      Keywords

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      References

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        Challenges in predicting protein-protein interactions from measurements of molecular diffusivity.
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        Rapid quantification of protein particles in high-concentration antibody formulations.
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        Deep convolutional neural network analysis of flow imaging microscopy data to classify subvisible particles in protein formulations.
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