个人简介
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
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
研究领域
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.
近期论文
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Guest sequence can influence RNA encapsulation by an engineered cationic protein capsid.
Fu J, Woycechowsky KJ. Biochemistry 2020, 59, 1517-1526. doi: 10.1021/acs.biochem.0c00077
A protein capsid-based system for cell delivery of selenocysteine.
Wang S, Al-Soodani AT, Thomas GC, Buck-Koehntop B, Woycechowsky KJ. Bioconjugate Chemistry 2018, 29, 2332-2342. doi:10.1021/acs.bioconjchem.8b00302.
Encapsulation and controlled release of protein guests by the Bacillus subtilis lumazine synthase capsid.
Han X, Woycechowsky KJ. Biochemistry 2017, 56, 6211-6200. doi:10.1021/acs.biochem.7b00669.
Reversible loading of thiol-modified curcumin in an engineered protein capsid.
Guo Q, Thomas GC, Woycechowsky KJ. RSC Adv 2017, 7, 34676-34686. doi:10.1039/C7RA05890J.
In vivo encapsulation of nucleic acids using an engineered nonviral protein capsid.
Lilavivat S, Sardar D, Jana S, Thomas GC, Woycechowsky KJ. J Am Chem Soc 2012, 134, 13152-13155. doi:10.1021/ja302743g.
Conversion of a dodecahedral protein capsid into pentamers via minimal point mutations.
Chen HN, Woycechowsky KJ. Biochemistry 2012, 51, 4704-4712. doi:10.1021/bi3003555.
Reagentless oxidative folding of disulfide-rich peptides catalyzed by an intramolecular diselenide.
Steiner AM, Woycechowsky KJ, Olivera BM, Bulaj G. Angew Chem Int Ed Engl 2012, 51, 5580-5584. doi:10.1002/anie.201200062.
Directed evolution of a protein container.
Wörsdörfer B, Woycechowsky KJ, Hilvert D. Science 2011, 331, 589-592. doi:10.1126/science.1199081.
Diselenides as universal oxidative folding catalysts of diverse proteins.
Beld J, Woycechowsky KJ, Hilvert D. J Biotechnol 2010, 150, 481-489. doi:10.1016/j.jbiotec.2010.09.956.
Small-molecule diselenides catalyze oxidative protein folding in vivo.
Beld J, Woycechowsky KJ, Hilvert D. ACS Chem Biol 2010, 5, 177-182. doi:10.1021/cb9002688.
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