Zhaohui "Sunny" Zhou
Faculty Fellow, Barnett Institute
Associate Professor of Chemistry & Chemical Biology
The Barnett Institute
341 Mugar Life Sciences Building
360 Huntington Avenue
Boston MA 02115
Professor Zhaohui Sunny Zhou, who joined the Barnett in Jan 2007, applies organic chemistry, analytical chemistry and protein engineering to biology and medicine. One program is to devise new methodologies to characterize protein post-translational modifications, such as S-adenosylmethionine-dependent methylations and protein processing via proteolysis. In addition, a general strategy is envisioned to selectively decorate proteins, such as protein drugs, using a combination of engineered enzymes with tailored sequence specificity and chemical modifications with functional selectivity. A second program area is the mechanistic study of biologically important enzymes, towards the design and synthesis of inhibitors. Current targets include several pathways involved in bacterial communication and biofilm formation, a major clinical problem with no effective treatment.
Professor Zhaohui Zhou (pronounced like Joe), a.k.a. Sunny, received his B.S. in chemistry in 1990 from the Department of Chemistry at Peking University, Beijing, China. He then worked for a year on natural products at the Academy of Traditional Chinese Medicine and Materia Medica, Changchun, Jilin, China. In 1997, he received his Ph.D. in bioorganic chemistry from the Scripps Research Institute under Professor Donald Hilvert in the Departments of Chemistry and Molecular Biology. He did postdoctoral research with Professor Rowena G. Matthews in the Biophysics Research Division and Department of Biological Chemistry at the University of Michigan, Ann Arbor. From 2000, he was an Assistant Professor in the Department of Chemistry at Washington State University, and also held appointments at the School of Molecular Biosciences, the Graduate Program of Pharmacology and Toxicology, and the NIH Biotechnology Training Program on Protein Chemistry. He joined the Barnett Institute in January 2007.
PRMT1 Demonstrates Primary Amino Acid Sequence Selectivity: Discrimination of Substrates and Altered Product Formation. Whitney L. Wooderchak, Tianzhu Zang, Zhaohui Sunny Zhou, Marcela Acuña, Stanley M. Tahara, Joan M. Hevel, Biochemistry, 2008, 47, 9456-66. pubmed
Chemo-enzymatic detection of protein isoaspartate using protein isoaspartate methyltransferase and hydrazine trapping. Alfaro JF, Gillies LA, Sun HG, Dai S, Zang T, Klaene JJ, Kim BJ, Lowenson JD, Clarke SG, Karger BL, Zhou ZS. Anal Chem. 80(10):3882-9 (2008) pubmed
An enzyme-coupled continuous spectrophotometric assay for S-adenosylmethionine-dependent methyltransferases. Dorgan KM, Wooderchak WL, Wynn DP, Karschner EL, Alfaro JF, Cui Y, Zhou ZS, Hevel JM. Anal Biochem. 2006 Mar 15;350(2):249-55. pubmed
Synthesis of LuxS inhibitors targeting bacterial cell-cell communication. Alfaro JF, Zhang T, Wynn DP, Karschner EL, Zhou ZS. Org Lett. 2004 Sep 2;6(18):3043-6. pubmed
Rapid screening for S-adenosylmethionine-dependent methylation products by enzyme-transferred isotope patterns analysis. Wan W, Zhao G, Al-Saad K, Siems WF, Zhou ZS. Rapid Commun Mass Spectrom. 2004;18(3):319-24. pubmed
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