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University of Colorado Denver

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John Carpenter, PhD

Professor of Pharmaceutical Sciences and Co-Director of the Center for Pharmaceutical Biotechnology


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Mailing address:

University of Colorado School of Pharmacy
Mail Stop C238
12850 E. Montview Blvd. V20-4119
Aurora, CO 80045

Office Location:

Pharmacy and Pharmaceutical Sciences Building (V20)
Fourth Floor
Room 4119

Lab Location:

Pharmacy and Pharmaceutical Sciences Building (V20)
Fourth Floor
Room 4430A/D

Contact:

Affiliation

  • Co-Director, Center for Pharmaceutical Biotechnology

Training and Education:

  • BS, Duke University (Zoology)
  • MS, Oregon State University (Zoology)
  • PhD., University of Southwest Louisiana (Biology)

Research Interest:

Proteins are becoming increasingly important as therapeutic agents. Due to their inherent instability, proteins present a unique challenge in the development of stable formulations. We study the mechanisms by which proteins are damaged in liquid and dried formulations, and the mechanisms by which additives inhibit this damage.  Our work on protein aggregation includes not only studies on therapeutic proteins, but also investigations into the amyloid fibril formation by proteins involved in human diseases such as systemic amyloidosis and Parkinson's disease. In addition, we are studying the use of high hydrostatic pressure to disaggregate and refold proteins.

Teaching

  • Professional Program: Physiology, Pathophysiology
  • Graduate Program: Protein Chemistry, Spectroscopic Analysis of Biomolecules

Representative Publications:

  • Roy, S., R. Jung, B.A. Kerwin, T.W. Randolph and J.F. Carpenter, 2005. Effects of benzyl alcohol on aggregation of recombinant human interleukin-1-receptor antagonist in reconstituted lyophilized formulations. J. Pharm. Sci. 94:382-396. 
  • Garzon-Rodriguez, W., R.L. Koval, S. Chongprasert, S. Krishnan, T.W. Randolph, N.W. Warne and J.F. Carpenter, 2004. Optimizing storage stability of lyophilized recombinant human interleukin-1 with disaccharide/hydroxyethyl starch mixtures.  J. Pharm. Sci. 93:684-696.
  • Chi, E.Y., S. Krishnan, B.S. Kendrick, B.S. Chang, J.F. Carpenter and T.W. Randolph, 2003. Roles of conformational stability and colloidal stability in the aggregation of recombinant human granulocyte colony-stimulating factor. Protein Science 12:903-913.
  • S. Krishnan, E.Y. Chi, S.J. Wood, B.S. Kendrick, C. Li, W. Garzon-Rodriguez, J. Wypych, T.W. Randolph, L.O. Narhi, A.L. Biere, M. Citron and J.F. Carpenter, 2003. Oxidative dimer formation is the critical rate-limiting step for Parkinson's disease alpha-synuclein fibrillogenesis. Biochemistry  42:829-837.
  • Kim, Y.S. T.W. Randolph, M.C. Manning, F.J. Stevens and J.F. Carpenter, 2003. Congo red populates partially unfolded States of an amyloidogenic protein to enhance aggregation and amyloid fibril formation. J. Biol. Chem. 278:10842-10850