TJU HEALTH SCIENCES PLATFORM

Introduction

Kenneth Woycechowsky——Professor
Nationality:	USA
Phone:	022-27401021
Email:	kenneth@tju.edu.cn
Office:	Room A505, Building 24, Tianjin University
School:	School of Pharmaceutical Science and Technology
ResearcherID:	K-5833-2015
Group weblink
	http://woycechowskylab.website2.me/

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

Patents

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
2000	Native disulfide bond formation in proteins	Woycechowsky, KJ; Raines, RT	Current Opinion in Chemical Biology	4
1999	A small-molecule catalyst of protein folding in vitro and in vivo	Woycechowsky, KJ; Wittrup, KD; Raines, RT	Chemistry & Biology	6
	Resin used for oxidative protein, e.g. ribonuclease A folding, comprises water-compatible polymer, and diselenide compound covalently bound to polymer by linker	HILVERT D; BELD J; WOYCECHOWSKY K J
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Kenneth Woycechowsky——Professor

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