Kenneth Woycechowsky
School
School of Pharmaceutical Science and Technology
Professional Title
Associate professor
Contact Information
022-27401021
kenneth@tju.edu.cn
Room A505, Building 24, Tianjin University
Education Background
- Postdoctoral| ETH-Zürich, CH| Organic Chemistry | 2019
- Ph. D. | University Wisconsin-Madison, WI, USA| Biochemistry | 2019
Research Interests
- Research projects in our lab fall into three main areas, including 1) capsid self-assembly, 2) molecular encapsulation, and 3) drug delivery.
- 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.
- 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.
- 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.
Positions & Employments
-
2019.12-2019.12
School of Pharmaceutical Science and Technology, Tianjin University | Professor -
2019.12-2019.12
Department of Chemistry, University of Utah | Assistant Professor
Academic Achievements
- Books
- [1] 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.
- [2] Chen, H.-N.; Woycechowsky, K. J. Conversion of a dodecahedral protein capsid into pentamers via minimal point mutations. Biochemistry 2012, 51, 4704.
-
- [3] 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.
- [4] 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.
- [5] Wörsdörfer, B.; Woycechowsky, K. J.; Hilvert, D. Directed evolution of a protein container. Science 2011, 331, 589.
- Honors & Awards
- [1] National Institutes of Health postdoctoral fellowship, 2004-2006
- [2] NIH Chemistry-Biology Interface training grant, 1995-1998
-
- [3] Wisconsin Alumni Research Foundation fellowship, 1994-1995
- [4] National Institutes of Health postdoctoral fellowship, 2004-2006
- [5] NIH Chemistry-Biology Interface training grant, 1995-1998
- [6] Wisconsin Alumni Research Foundation fellowship, 1994-1995
- [7] National Institutes of Health postdoctoral fellowship, 2004-2006
- [8] NIH Chemistry-Biology Interface training grant, 1995-1998
- [9] Wisconsin Alumni Research Foundation fellowship, 1994-1995