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杨科武
5.0我来评喜爱度
所在大学:西北大学
所在院系:化学系
所在地区:陕西
所在城市:西安
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杨科武老师介绍
杨科武 性别:男
部门:有机化学与化学生物学学部
职称:教授/博士生导师
邮箱:kwyang@nwu.edu.cn 电话: Phone/Fax: +86/0-29-8830-2429(O)
研究方向: Chemical Biology, Metalloenzyme & Antibiotic Resistance, ProteinChip, Biopharmaceuticals
简 介
Biography
Professor Yang received his Ph.D. in chemistry in 1994 from Lanzhou Institute of Chemical Physics, Chinese Academy of Sciences, working under the supervision of Yuanqi Yin. He spent the following two years as a national post-doctoral fellow and then joined the faculty at Fudan University as an associate professor in 1997. He was invited to pursue National Institutes of Health's research projects at Miami University working in the lab of Michael Crowder from 1998 to 2004, and then serviced Girindus America Inc. at Department of Medicinal Chemistry as a senior scientist to mastermind R&D projects of Procter & Gamble and Aventis pharmaceuticals. Professor Yang joined the faculty at Northwest University as a professor and leading investigator in chemical biology in 2007. He is a member of SIGMA XI, The Scientific Research Society.
Research Interests
My research focuses on important biomedical targets. We are interested in using the tools of protein chemistry, organic synthesis, molecular biology and biophysics to develop clinically-useful compounds for diagnoses and treatment of the biomedical targets including antibiotic resistant bacteria. We are particularly interested in taking a multidisciplinary approach to develop a ProteinChip technology for high throughput screening of the antibiotic resistant bacteria. Researchers in the group work at the interface of chemistry, biology, medicine and pharmaceuticals. We are currently engaging the following projects.
1. Diagnoses of the Antibiotic Resistant Bacteria
The most common and most often prescribed antibiotics are β-lactam-containing compounds such as penicillin, cephalosporin, cephamycin, and carbapenem families. The β-lactam-containing antibiotics exhibit their antimicrobial activity by inactivating bacterial transpeptidases, which are enzymes required for bacterial cell wall synthesis. The inactivation of transpeptidase results in a weakened bacterial cell wall which is susceptible to osmotic lysis. The overuse of antibiotics in the clinical setting has resulted in a large number of bacteria which are resistant to most or all commonly-used antibiotics. The most common way for bacteria to become resistant to β-lactam-containing antibiotics is to produce an enzyme called metallo-β-lactamase, which have been shown to bind 1-2 Zn(II) ions per monomer and hydrolyze all tested β-lactam-containing antibiotics. We are currently conducting structural and mechanistic characterization of the metallo-β-lactamases from S. maltophilia (L1), A. sobria (ImiS), and B. fragilis (CcrA) using NMR, EPR, EXAFS, RFQ and molecular biology technology in an attempt to develop a specific compound for diagnoses of the antibiotic resistant bacteria, and to develop potential inhibitors of the target enzymes to combat infection of the antibiotic resistant bacteria.
2. Antibiotic Resistance in Bacteria --- D-ala-D-ala-Dipeptidase VanX
Vancomycin inhibits bacterial cell wall synthesis by binding to the D-ala-D-alanine end of the pentapeptide via five hydrogen bonds, thereby preventing cross-linking of the pentapeptides to form the normal bacterial peptidoglycan layer. VanX hydrolyzes all or most of D-ala-D-alanyl dipeptides of the pentapeptides so that vancomycin loses the targets. Clearly, to produce tight-binding inhibitor of VanX is an effective way to combat vancomycin resistance in bacteria. Towards this goal, we are implementing a rational strategy to design, synthesize and evaluate inhibitors of the target enzyme, to investigate structure-activity relationship (SAR) of the inhibitors, which is used for guiding design of new drugs, and hopefully to obtain a compound for clinic purpose.
3. Inhibition Studies on Glyoxalase-II Isozymes from A. thaliana
Biochemical studies on glyoxalase system have implicated Glyoxalase-II (GLX-II) is in detoxification of cytotoxic 2-oxoaldehydes from the cell and several groups have reported that inhibitors of GLX-II can stop growth of tumors, because the tumors have no way to remove the toxic byproducts. In this project, we have demonstrated that the GLX-II from A. thaliana binds two atoms of Zn/monomer. In an effort to probe inhibition of GLX-II, we systematically design, synthesize and evaluate glutathione derivatives as inhibitors, and investigated which substitutes on the inhibitor are essential for tight binding, whether hydrophobic interactions contribute to the tight binding of the inhibitors and whether entropic effects explain the tight binding of the inhibitors. This study is targeted for development of potential anti-tumor reagents.
4. ProteinChip and Small Molecule Chip
Based on our deep understanding and investidating to structures, mechanism, functions and inhibition of the metalloenzymes in antibiotic resistant bacteria and their reaction with specific substrates and inhibitors, we are taking a multidisciplinary approach to develop a specific ProteinChip technology for detecting the antibiotic resistant bacteria, and to develop a specific Small Molecule Chip technoloty for high throughput screening of antibacterial reagents.
Main Projects Accomplished
* Development of Prodrugs for the Treatment of Osteoporosis, Procter & Gamble, PI
* Synthetic Development of Anti-herpes Compounds, Aventis Pharmaceuticals, PI
* Characterization of Metallo-β-lactamases, National Institutes of Health (NIH), Co-PI
* Characterization of Metallo-β-lactamases from X. maltophilia, NIH, Co-PI
* Inhibition Studies on D-ala-D-ala Dipeptidase VanX, NSF, Co-PI
* Studies on Glyoxalase II in Arabidopsis thaliana, National Science Fundation, Co-PI
Offering Courses at NWU
* Foundations of Chemical Biology
* Biochemistry
* Principles of Bioinorganic Chemistry
Selected Publications
* Mechanistic Studies on the Mononuclear Zn(II)-Containing Metallo-β-Lactamase ImiS from Aeromonas Sobria, Biochemistry, 45, 10729-10738, 2006.
* X-ray Absorption Spectroscopy of the Zinc-Binding Sites in the Class B2 Metallo-β-lactamase ImiS from Aeromonas veronii bv. Sobria, Biochemistry, 45, 13650-13658, 2006.
* Sequential Binding of Cobalt(II) to Metallo-β-Lactamase CcrA, Biochemistry, 45, 1313-1320, 2006.
* Site Selective Binding of Zn(II) to Metallo-β-Lactamase L1 from Stenotrophomonas Maltophilia, J. Biol. Inorg. Chem. 11(3), 351-358, 2006.
* Spectroscopic Studies on Co(II)-Substituted Metallo-β-Lactamase ImiS from Aeromonas veronii bv. Sobria, Biochemistry, 44, 5168-5176, 2005.
* Structural Studies on a Mitochondrial Glyoxalase II, J. Biol. Chem. 280, 40668-40675, 2005.
* Phosphinate, Sulfonate and Sulfonamidate Dipeptides as Potential Inhibitors of Aminopeptidase N, Bioorg. Med. Chem. Lett. 15, 5150-5153, 2005.
* A Method for Removing Ethylenediaminetetraacetic Acid from Apo-proteins, Anal. Biochem. 329, 342-344, 2004.
* Explaining the Inhibition of Glyoxalase II by 9-Fluorenylmethoxycarbonyl-protected Glutathione Derivatives, Arch. Biochem. Biophys, 414, 271-278, 2003.
* The Problem of a Solvent Exposable Disulfide when Preparing Co(II)-Substituted Metallo-β-Lactamase L1 from Stenotrophomonas maltophilia, J. Biol. Inorg. Chem. 6, 91-99, 2001.
Help Yourself
ABB_321.pdf
ABB_918.pdf
JBIC_120.pdf
BIOCHEM_629.pdf
BMCL_019.pdf
JBIC_627.pdf
BMCL_525.pdf
BIOCHEM_524.pdf
Mailing Address
Dr. Kewu Yang
Department of Chemistry
Northwest University
229 North Taibai Road
Xi'an, Shaanxi 710069, PR China
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