Home / People / / Kenneth Woycechowsky

Kenneth Woycechowsky——Professor

Room A505, Building 24, Tianjin University
School of Pharmaceutical Science and Technology
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Education Experience
1994-2002 Ph. D. Biochemistry University Wisconsin-Madison, WI, USA
2002-2008 Postdoctoral Organic Chemistry ETH-Zürich, CH
Professional Experience
2008-2014 Assistant Professor Department of Chemistry, University of Utah
2014- Professor School of Pharmaceutical Science and Technology, Tianjin University
Research Area

The research in the Woycechowsky group focuses on the supramolecular chemistry of proteins. In particular, we are interested in proteins that assemble into symmetrical, closed-shell, polyhedral capsid structures. Protein capsids can act as molecular containers and delivery vehicles for a variety of molecular cargoes, and therefore are useful for bionanotechnological applications, such as drug delivery, catalysis, and materials synthesis. Protein engineering strategies are used to explore and exploit the supramolecular chemistry of protein capsids. This approach is inherently interdisciplinary, utilizing methods from biochemistry, biophysics, molecular biology, organic chemistry, and cell biology. Research projects in our lab fall into three main areas, including 1) capsid self-assembly, 2) molecular encapsulation, and 3) drug delivery.


Honors and Awards
National Institutes of Health postdoctoral fellowship, 2004-2006
NIH Chemistry-Biology Interface training grant, 1995-1998
Wisconsin Alumni Research Foundation fellowship, 1994-1995
Beld, J.; Woycechowsky, K.J.; and Hilvert, D. Diselenide resins for oxidative protein folding. European Patent Office application number EP09013216 (2009).
Highlighted Publications
Lilavivat, S.; Sardar, D.; Jana, S.; Thomas, G. C.; Woycechowsky, K. J. In Vivo encapsulation of nucleic acids using an engineered non-viral protein capsid. J. Am. Chem. Soc. 2012, 134, 13152.
Chen, H.-N.; Woycechowsky, K. J. Conversion of a dodecahedral protein capsid into pentamers via minimal point mutations. Biochemistry 2012, 51, 4704.
Steiner, A.M.; Woycechowsky, K. J.; Olivera, B. M.; Bulaj, G. Reagentless oxidative folding of disulfide-rich peptides is catalyzed by an intramolecular diselenide. Angew. Chem., Int. Ed. 2012, 51, 5580.
Wörsdörfer, B.; Woycechowsky, K. J.; Hilvert, D. Directed evolution of a protein container. Science 2011, 331, 589.
Woycechowsky, K. J.; Choutko, A.; Vamvaca, K.; Hilvert, D. Relative tolerance of an enzymatic molten globule and its thermostable counterpart to point mutation. Biochemistry 2008, 47, 13489.
ResearcherID Publications
Year Title Author(s) Source Volume
2007 Novel enzymes through design and evolution. Woycechowsky, Kenneth J; Vamvaca, Katherina; Hilvert, Donald Advances in enzymology and related areas of molecular biology 75
2007 Selenoglutathione: Efficient oxidative protein folding by a diselenide Beld, Joris; Woycechowsky, Kenneth J.; Hilvert, Donald Biochemistry 46
2006 A simple tagging system for protein encapsulation Seebeck, FP; Woycechowsky, KJ; Zhuang, W; et al. Journal of the American Chemical Society 128
2006 Tunnel plasticity and quaternary structural integrity of a pentameric protein ring Woycechowsky, KJ; Seebeck, FP; Hilvert, D Protein Science 15
2004 Deciphering enzymes - Genetic selection as a probe of structure and mechanism Woycechowsky, KJ; Hilvert, D European Journal of Biochemistry 271
2004 Recombination of fragmented proteins Woycechowsky, KJ Chemistry & Biology 11
2003 Catalysis of protein folding by an immobilized small-molecule dithiol Woycechowsky, KJ; Hook, BA; Raines, RT Biotechnology Progress 19
2003 The CXC motif: A functional mimic of protein disulfide isomerase Woycechowsky, KJ; Raines, RT Biochemistry 42
2000 A highly active immobilized ribonuclease Sweeney, RY; Kelemen, BR; Woycechowsky, KJ; et al. Analytical Biochemistry 286
2000 Contribution of disulfide bonds to the conformational stability and catalytic activity of ribonuclease A Klink, TA; Woycechowsky, KJ; Taylor, KM; et al. European Journal of Biochemistry 267
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