个人简介
Degrees:
2003 Ph.D., Biochemistry, Princeton University, Princeton, NJ.
1998 M.Sc., Analytical Chemistry, Peking University, Beijing, China.
1996 B.Sc., Analytical Chemistry, Peking University, Beijing, China.
2008-
Assistant Professor, Chemistry Department,
University of Kentucky
2007
Research Assistant Professor, Chemistry Department,
University of Kentucky.
2006
Postdoctoral Research Associate, Chemistry Department,
University of Kentucky. (Mentor: Dr. Leonidas G. Bachas)
2003-2006
Goldhaber Research Fellow, Biology Department,
Brookhaven National Laboratory. (Mentor: Dr. Dax Fu)
1998-2003
Graduate student, Department of Chemistry, Princeton University.
(Advisor: Dr. Michael H. Hecht)
1996-1998
Graduate student, Department of Chemistry, Peking University.
(Advisor: Prof. Yuanzong Li)
1991-1996
Undergraduate student, Department of Chemistry, Peking University.
(Advisor: Prof. Yuanzong Li)
研究领域
Fighting the war against multi-drug resistant bacteria through the study of the bacteria multi-drug resistance transporter protein
The emergence of multi-drug resistant bacteria, immune to all known antibiotics, is a severe threat to human health. These super bugs gain multi-
4. Viral capsid-based particles as cancer targeting drug delivery vesicles and nanoscale bioinorganic building blocks
The quest for new nano-sized chemical architecture has promoted an interest in utilizing existing biogenic assemblies of the proper dimension, such as viruses. Viruses consist of two components, a nucleic acid genome, where the hereditary information is stored, surrounded by a protective shell of protein called the capsid. Virus capsids have emerged as versatile tools in multiple aspect of nano-technology applications, serving as scaffolds or building blocks for novel materials, nano-sized reactors, well-controlled chemical reactions, or as containers for specific labels in diagnostic imaging. We are interested in using viral protein capsid as a model to develop viral capsid-based tools. This technology has potential application in targeted drug delivery, histological tumor-typing assays, and in making nanoscale building blocks with an integrated inorganic coat or core for the construction of novel biomaterials.
The interaction between protein and DNA is critical to life and is usually regulated by a third species, an effector. We are interested in coupling such interactions with nanoparticle assembling to construct smart materials as well as convenient sensing systems. As a proof-of-principle experiment, we have demonstrated that lac repressor (the protein, ribbons in panel A) mediated the aggregation of gold nanoparticles (AuNPs) modified using lac operator (the DNA, space filled model in panel A). Furthermore, the presence of a small molecule effector (IPTG) prevented the particles from aggregate. In panel B, cuvette 1, 2, and 3 contain lac operator-modified AuNP (LacO-AuNP), LacO-AuNP plus lac repressor, and LacO-AuNP plus lac repressot and IPTG.particle plus protein and IPTG, respectively.
drug resistance (MDR) mainly through up-regulating the expression of multi-drug efflux
pumps. These pumps are membrane transporter proteins that recognize a broad spectrum of structurally different compounds and actively pump these compounds out of the cell. We are investigating the structure, function and folding of these proteins with the long term goal of finding approaches to disable the MDR pumps.
The expression of the MDR pumps is regulated by a group of regulator proteins. We are also studying the MDR regulators and their interplay with DNA and small molecule effectors, aiming at discovering tools to break the chain of regulation that lead to MDR pump over-expression.
Structure of AcrB
A MDR regulator, ST1710, from a thermophile senses the presence of small drug ligands and binds to/releases from its cognate DNA binding site accordingly.
2. Nanoparticle assembly mediated by protein-DNA interaction.
A
B
1 2 3
AFM characterization of lacOS-AuNPs alone (A), in the presence of the lac repressor (B) and in the presence of the lac repressor plus IPTG (C). Both AuNPs (bright orange) and proteins (green) are visible in (B) and (C). All images are representative topography images and are rendered in the same 50 nm height scale.
5. Developing sensors for biomarkers
We are interested in developing biosensing platforms for the detection of biomarkers and drugs. Such platforms are based on the recognition between biomacromolecules and their specific ligands. Keywords in our design include aptamers, fluorescence, and site-specific and reversible protein immobilization.
Green fluorescence protein (GFP) is site-specifically immobilized to sepharose resins (A, left). The green color is apparent compared to the control sample (A, right). B, Picture of GFP modified resin taken using fluorescence microscope.
近期论文
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Lu W., Zhong M., Wei Y.* 2011. “A reporter platform for the monitoring of in vivo conformational changes in AcrB” Prot. Pep. Lett. 18, 863-71.
Fang J., and Wei Y.* 2011. “A small globular protein motif forms particulate hydrogel under various pH conditions” Biomacromolecules, 12, 1578–1584.
Fang J., and Wei Y.* 2011. “Expression, purification and characterization of the Escherichia coli integral membrane protein YajC” Prot. Pep. Lett. 18, 601-608.
Deo S., Wei Y., Daunert S.* 2012. Probing a myth: does the younger generation of scientists have it easier? Anal. Bioanal. Chem. 403, 2065-2067.
Geng S., Fang J., Turner K., Daunert S., Wei Y.* 2012, “Accumulation and efflux of polychlorinated biphenyls in Escherichia coli” Anal. Bioanal. Chem. 403, 2403-2409.
Fang J., Zhang X., Clements W. H., Chai Q., Cai Y., Wei Y.* 2012, “Noncovalent interactions in YajC-CT fibrillation and gelation-effects of detergent, urea, salt, and glycerol” J. Biol. Res. 1: 53.
Lu W., Chai Q., Zhong M., Yu L., Wang T., Li H., Zhu H., and Wei Y.* 2012. “Assembling of AcrB trimer in cell membrane” J. Mol. Biol. 423:123-134.
Knecht L. D., Ali N., Wei Y., Hilt J. Z., Daunert S.* 2012, “Nanoparticle-mediated remote control of enzymatic activity” ACS Nano, 6: 9079–9086.
Yewle J. N., Wei Y., Puleo D. A., Daunert S., and Bachas L. G.* 2012, “Oriented immobilization of proteins on hydroxyapatite surface using bifunctional bisphosphonates as linkers” Biomacromolecules. 13: 1742-1749.
Nehru N., Donev E. U., Huda G. M., Yu L., Wei Y., Hastings J. T.* 2012, “Differentiating surface and bulk interactions using localized surface plasmon resonances of gold nanorods” Optics Express, 20: 6905-6914.
Fang J., Yu L., Wu M., and Wei Y.* 2013. “Dissecting the function of a protruding loop in AcrB trimerization” J. Biomolecular Structure Dynamics. 31:385-92.
Baker N. A., Karounos M., English V., Fang J., Wei Y., Stromberg A., Sunkara M., Morris A. J., Swanson H. I., Cassis L. A.* 2013, "Coplanar polychlorinated biphenyls impair glucose homeostasis in lean C57BL/6 mice and mitigate beneficial effects of weight loss on glucose homeostasis in obese mice" Env. Health Perspect. 121(1):105-10.
Ye C., Chai Q., Zhong M., and Wei Y.* 2013. “Effect of crowding by Ficolls on OmpA and OmpT membrane insertion” Protein Sci. 22(2):239-45.
Zhong M, Ferrell B., Lu W., Chai Q., and Wei Y.* 2013. “Structural flexibility and SurA activity—insight into the function of a periplasmic molecular chaperone” J. Bacteriol. 195(5):1061-7.
Yu L., Zhong M., Lu W., Ye C., Chai Q., Sheetz M., and Wei Y.* 2013. “Role of a conserved residue R780 in Escherichia coli multidrug transporter AcrB” Biochemistry. 52(39): 6790-6.
Chai Q., Ferrell B., Zhong M., Zhang X., Ye C., Wei Y.* 2014. “Diverse sequences are functional at the C-terminus of the E. coli periplasmic chaperone SurA” PEDS 27(4):111-6.
Lu W., Zhong M., Chai Q., Wang Z., Yu L., Wei Y.* 2014. “Functional relevance of AcrB trimerization in pump assembly and substrate binding” PLoS One 9, e89143.
Ye C., Wang Z., Lu W., Wei Y.* 2014. “Unfolding study of trimeric membrane protein AcrB” Protein Sci. [Online early access] 620 DOI: 10.1002/pro.2471, Published Online: April 17.
Nehru N., Yu L., Wei Y., and Hastings J. T.* 2014. “Using U-shaped localized surface plasmon resonance sensors to compensate for nonspecific interactions”. IEEE T Nanotechnol. 13 (1): 55-61
Ye C., Wang Z., Lu W., Zhong M., Chai Q., and Wei Y.* 2014. “Correlation between AcrB Trimer Association Affinity and Efflux Activity”. Biochemistry, Just Accepted Manuscript DOI: 10.1021/bi5000838 Publication Date (Web): May 22, 2014
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