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Research Group of Professor Hiroshi Matsui at Hunter College

Research Interests:
Bio-Nanotechnology, Electronics, Sensors, Photonics, Spectroscopy

Attention : POSTDOCTORAL POSITION AVAILABLE (Electrochemistry, Solution-phase AFM, Bionanotechnology, Nanocrystals)


Research Description:

1. Biomimetic Fabrication of Nano-Electronics

2. Engineering New Peptide Nanowires from Nature

3. Bio-Sensor Chips Engineered by Peptide Nanowires

4. Scanning Probe Microscopy-Based Nanolithography for Biomolecular Patterning

Publications

Current Group Members

1. Biomimetic Fabrication of Nano-Electronics

Our fabrication strategy consists of two crucial steps; Self-Assembly of Nanoscale Building Blocks into Device Designs and Biomimetic Crystal Growth of Metals and Semiconductors with Catalytic Activity.

Self-Assembly of Nanoscale Building Blocks into Device Designs

Non-lithographic fabrications of devices such as electronics, photonics, and sensor have been studied extensively by assembling nanometer-sized building blocks into the device configurations. While various nanowires and nanoparticles with superior physical properties have been synthesized as the building blocks, more reproducible methods to assemble them onto precise positions are desirable to construct the nanodevices. We have been fabricating peptide-based nanotubes and functionalizing them with various recognition components (antibody), and our strategy is to use those functionalized peptide nanotubes, which can recognize and selectively bind a well-defined region on antigen-patterned substrates, as building blocks to assemble three-dimensional nanoscale architectures at uniquely defined positions (Figure 1). Recently, our idea for this biologically programmed assembly of nanomaterials was recognized as the Most-Accessed Article in the year of 2007 in Journal of the American Chemical Society (JACS)
(
http://pubs.acs.org/journals/jacsat/promo/most/most_accessed/index.html).

Fig1

Figure 1. Illustrations and images of our antibody nanotube array fabrication examples. (a) SEM image of avidin-coated nanotubes interconnecting two Au electrodes labeled by biotin and its illustration (b) (Left) Scheme to assemble anti-mouse IgG-coated nanotubes and anti-human IgG-coated nanotubes onto their antigen-patterned substrates via biomolecular recognition; Location-specific immobilization of Alexa Fluor 546-labeled anti-mouse IgG nanotubes onto the mouse IgG trenches and FITC-labeled anti-human IgG nanotubes onto the human IgG trenches. (Center) Fluorescence image of anti-mouse IgG nanotubes (red) and anti-human IgG nanotubes (green), attached onto four upper trenches filled with mouse IgG and four bottom trenches filled with human IgG, respectively, scale bar = 2 mm.  (Right) Locations of human-IgG and mouse-IgG arrays. (c) (Left) Scheme to assemble two different antibody nanotubes, anti-mouse IgG-coated nanotube and anti-human IgG-coated nanotube, into the cross-bar geometry by biomolecular recognition. (Right) AFM image of these two antibody nanotubes assembled in the cross-bar geometry. Scale bar = 200 nm. [I.A. Banerjee, L. Yu, H. Matsui, Nano Lett., 3, 283 (2003), Z. Zhao, I.A. Banerjee, H. Matsui, J. Am. Chem. Soc., 127, 8930 (2005), L. Yang, N. Nuraje, H. Bai, H. Matsui, J. Pep. Sci., 14, 203 (2008)]

 Biomimetic Crystal Growth of Metals and Semiconductors with Catalytic Activity

Even though those antibody-incorporated nanomaterials can be immobilized at desired locations by the biomolecular recognition, their electric properties are necessary to be adjusted to function as building blocks for electric or sensor devices. Therefore, after configuring device geometries with these nanotubes by the biomolecular recognition, we turned on the biomineralization function of peptides on the nanotube sidewall to coat with various materials such as metals, semiconductors, and quantum dots for electronics, photonics, and sensor applications. The coating morphology such as particle-domain size and inter-particle distance on the nanotubes could be tuned by peptide sequences and conformations (Figure 2). Since the particle-domain size and the inter-particle distance determine the electric property of the coated nanotube, this bionanotubes serve as a very smart template whose electronic property and band gap could be tunable by simply adjusting the conformation of mineralizing peptide on the nanotube surface. 

Combining the first part and the second part of technology, we are currently developing electric circuits and pathogen sensors.

Fig2

Figure 2. (a) Illustration of ZnS nanocrystal growth on the unfolding M1 peptides (VAL-CYS-ALA-THR-CYS-GLU-GLN-ILE-ALA-ASP-SER-GLN-HIS-ARG-SER-HIS-ARG-GLN-MET-VAL) on the template bolaamphiphile nanotubes as a function of pH. (b) Transmission electron micrograph (TEM) of wurtzite ZnS nanocrystals grown on the M1 peptide coated nanotubes at pH 5.5. Inset (left): Magnified ZnS nanocrystal TEM image. Inset (right): Electron diffraction (ED) pattern of ZnS nanocrystals indicating the wurtzite structure. scale bar = 70 nm.  [I.A. Banerjee, L. Yu, H. Matsui, J. Am. Chem. Soc., 127, 16002 (2005)]

 2. Genetically Engineering New Peptide Nanowires from Nature

Recently, we advanced our concept of the biomimetic device fabrication in the section 1 by applying collagen triple helices as new nanowire templates, whose chemical moiety, functionality and length could be controlled by using recombinant technology, such an expression system of collagen fragments in E. coli. Significant advantages of this system are to produce the biological wires with a uniform diameter (f = 4 nm) and a uniform length (controllable between 40 nm – 300 nm), and to produce them in a large quantity via cell amplification, both critical for the real-world applications (Figure 3). Slight modifications in peptide sequences of the triple helices via mutagenesis change their surface properties. When metals and semiconductors were grown on the triple helices as templates, their morphologies and dimensions were quite sensitive to the peptide sequences of the triple helix.

Fig3

Figure 3. Strategy to grow semiconductor nanowires at room temperature using triple helix peptide nanowires as catalytic templates. This peptide is a genetically modified collagen peptide whose mechanical strength is enhanced by recombinant technology. (a) TEM image of ZnO-coated triple helix nanowires. ZnO was grown even at 4 °C due to the peptide’s catalytic activity. (Inset) HRTEM image showing the single crystalline nature of ZnO. (b) Electron diffraction pattern of the resulting ZnO nanowires.   [H. Bai, K. Xu, Y. Xu, H. MatsuiI Angew. Chem. Intl. Ed., 46, 3319  (2007)]

3. Capacitance-based Bio-Sensor Chips Engineered by Peptide Nanowires

Traditionally, pathogens have been detected by either targeting microorganisms with labeled recognition elements or probing their nucleic acids or antigens with various labeling agents via optical detection, electrochemical measurement, or mechanical transduction. However, label-free detection of microorganisms is more advantageous due to its simple procedure without any further incubation steps, thus reducing costs and enabling fast detection. Although some prototypes for the label-free detection of bacterial cells have been proposed, examples of development of label-free detection systems for viruses are rather scarce mainly due to their nanometric dimensions and relatively inert nature against chemical treatments. Therefore, it remains a challenge to develop robust and label-free viral sensors which have extremely low detection limit in miniaturized chip configurations

Here we are developing two peptide nanotube-based methods to detect pathogens with scoring high on all of these sensing requirements. The first development is the antibody nanotube-based pathogen detection platform. In this platform, a pair of electrodes separated by a micrometric gap was bridged by antibody-coated peptide nanotubes, and the binding event between the virus and its antibody was detected by capacitance change between the electrodes (Figure 4). Due to the dielectric property of viruses, the binding of viruses with the antibody nanotubes decreased the permittivity of the surrounding medium, consequently decreasing the capacitance between the electrodes. By this method, herpes simplex virus type 2 (HSV-2) was detected in the concentration of 102 pfu/ml within one hour.

The second approach is to apply peptide nanotubes incorporating recognition units with antibodies at their ends and fluorescent signaling units at their sidewalls as signal enhancer for flow cytometry. Generally, nanoscale viruses are difficult to detect optically in the low detection limit due to the small size of viral structure. When viral pathogens were mixed with these antibody nanotubes in solution, the nanotubes rapidly aggregated around the viruses to form a networking structure and the size of the aggregates increased as the concentration of viruses increased. Trace quantities of viruses such as adenovirus, herpes simplex virus type 2 (HSV-2), influenza strain B, and vaccinia virus were detected on attomolar order by changes in fluorescence and light scattering intensities associated with aggregation of dye-loaded antibody nanotubes around viruses. High specificity of each antibody nanotube toward its targeted virus was demonstrated by quantifying concentrations of two different viruses in mixtures. This antibody nanotube assay allowed us to optically detect targeted pathogens in the trace levels within 30 minutes from the receipt of samples to the final quantitative data analysis.

Fig4

Figure 4. (top) Design of the antibody nanotube-based pathogen detection platform. The binding event between the virus and its antibody was detected by capacitance change between the electrodes. Due to the dielectric property of viruses, the binding of viruses with the antibody nanotubes decreased the permittivity of the surrounding medium, consequently decreasing the capacitance between the electrodes.
(bottom) Optical detection of pathogens with peptide nanotube markers. When viral pathogens were mixed with the antibody nanotubes in solution, the nanotubes rapidly aggregated around the viruses to form a networking structure and the size of the aggregates increased as the concentration of viruses increased. Trace quantities of were detected on attomolar order by changes in fluorescence and light scattering intensities associated with aggregation of dye-loaded antibody nanotubes around viruses. [R.I. MacCuspie, N. Nuraje, S-Y. Lee, A. Runge, and H. Matsui, J. Am. Chem. Soc., 130, 887 (2008), R.I. MacCuspie, I.A. Banerjee, S. Gummalla, H.S. Mostowski, P.R. Krause, and H. Matsui, Soft Matter, 4, 833 (2008)]

 A. Recent Publications (Bio-Nano)

  1. “Enzyme Urease as Nano-Reactor to Grow Crystalline ZnO Nanoshells at Room Temperature”, R. de la Rica and H. Matsui, Angew. Chem. Intl. Ed., 47, 5415 (2008).
  2. “Comparison of Electrical Properties of Viruses Studied by AC Capacitance Scanning Probe Microscopy”, R.I. MacCuspie, N. Nuraje, S-Y. Lee, A. Runge, and H. Matsui, J. Am. Chem. Soc., 130, 887 (2008).
  3. “Liquid/liquid interfacial epitaxial polymerization to grow single crystalline nanoneedles of various conducting polymers”, N. Nuraje, S. Kai, N.L. Yang and H. Matsui, ACS Nano, 2, 502 (2008).
  4. “Virus Assay Using Antibody-Functionalized Peptide Nanotubes”, R.I. MacCuspie, I.A. Banerjee, S. Gummalla, H.S. Mostowski, P.R. Krause, and H. Matsui, Soft Matter, 4, 833 (2008).
  5. ”Crossbar Assembly of Antibody-Functionalized Peptide Nanotubes via Biomimetic Molecular Recognition”, L. Yang, N. Nuraje, H. Bai, H. Matsui, J. Pep. Sci., 14, 203 (2008).
  6. “Fabrication of Au nanowire of uniform length and diameter using a new monodisperse and rigid biomolecular template, collagen-like triple helix”, H. Bai, K. Xu, Y. Xu, and H. Matsui, Angew. Chem. Intl. Ed., 46, 3319 (2007).
  7. “Catalytic growth of silica nanoparticles in controlled shapes at planar liquid/liquid interfaces”, N. Nuraje, K. Su, and H. Matsui, New J. Chem., 31, 1895 (2007).
  8. “Biomimetic and Aggregation-Driven Crystallization Route for Room-Temperature Material Synthesis: Growth of b-Ga2O3 Nanoparticles Using Peptide Assemblies as Nanoreactors”, S.Y. Lee, X. Gao, H. Matsui, J. Am. Chem. Soc., 129, 2954 (2007).
  9. “Single crystalline nanoneedles with fast conductance switching properties from an interfacial polymerization-crystallization of 3, 4-ethylenedioxythiophene”, K. Su, N. Nuraje, L. Zhang, I.W. Chu, R.M. Peetz, H. Matsui, and N-L. Yang, Adv. Mater., 19, 669 (2007).
  10. “Mineralization of semiconductor nanocrystals on peptide-coated bionanotubes and their pH-dependent morphology changes”, I.A. Banerjee, G. Muniz, S-Y. Lee, and H. Matsui, J. Nanosci. Nanotechnol, 7, 2287 (2007).
  11. “Fabrication of Magnetic Nanowires by Self-Assembling FePt Nanoparticles on Peptide Nanotubes”, L. Yu, P. Porrata, H. Matsui, ACS series, Self-Organized Photonic Materials, in print (2007).
  12. “Highly Accurate Immobilization of Antibody Nanotubes on Protein-Patterned Arrays with Their Biological Recognition by Tuning Their Ligand-Receptor Interactions”, Z. Zhao, H. Matsui, Small, 3, 1390 (2007).
  13. “Room Temperature-Synthesis of Ferroelectric Barium Titanate Nanoparticles Using Peptide Nano-Rings as Templates”, N. Nuraje, K. Su, A. Haboosheh, J. Samson, E.P. Manning, N-L. Yang, and H. Matsui, Adv. Mater., 18, 807 (2006).
  14. “Self-Assembly of Au Nanoparticle-Containing Peptide Nano-Rings on Surfaces”, N. Nuraje, K. Su, J. Samson, A. Haboosheh, R.I. MacCuspie and H. Matsui, Supramol. Chem., 18, 429 (2006). (the top 10 most accessed article in 2006 in Supramol. Chem.)
  15.  “Room-Temperature Wurtzite ZnS Nanocrystal Growth on Zn Finger-Like Peptide Nanotubes by Controlling Their Unfolding Peptide Structures”, I.A. Banerjee, L. Yu, and H. Matsui, J. Am. Chem. Soc., 127, 16002 (2005).
  16. “Peptide-Based Nanotubes and Their Applications in Bionanotechnology”, X. Gao, H. Matsui, Adv. Mater., 17, 2037 (2005).
  17. “Fabrication and Application of Enzyme-Incorporated Peptide Nanotubes”, L. Yu, I.A. Banerjee, X. Gao, N. Nuraje, H. Matsui, Bioconjugate Chem., 16, 1484 (2005).
  18. “Simultaneous Targeted Immobilization of Anti Human-IgG-Coated Nanotubes and Anti Mouse-IgG-Coated Nanotubes on the Complementary Antigen-Patterned Surfaces via Biological Molecular Recognition”, Z. Zhao, I.A. Banerjee, H. Matsui, J. Am. Chem. Soc., 127, 8930 (2005).
  19. “Simple Separation of Peptide Nanotubes by Using Size-Exclusion Columns and Fabrication of 1D Single-Chains of Au Nanoparticles on the Thin Peptide Nanotubes”, X. Gao, R. Djalali, A. Haboosheh, J. Samson, N. Nuraje, H. Matsui, Adv. Mater., 17, 1753 (2005).
  20. “Magnetic Nanotube Fabrication by Using Bacterial Magnetic Nanocrystals”, I.A. Banerjee, L. Yu, M. Shima, T. Yoshino, H. Takeyama, T. Matsunaga, H. Matsui, Adv, Mater., 17, 1128 (2005).
  21. “Controlled Growth of Se Nanoparticles on Ag Nanoparticles in Different Ratios”, X. Gao, L. Yu, R.I. MacCuspie, H. Matsui, Adv. Mater., 17, 426 (2005).
  22. “Thiolated Peptide Nanotube Assembly as Arrays on Patterned Au Substrates”, I.A. Banerjee, L. Yu, R.I. MacCuspie, H. Matsui, Nano Lett., 4, 2437 (2004).
  23.  “Attachment of Ferrocene Nanotubes on beta-CD Self-Assembled Monolayers with Molecular Recognitions”, Y-f Chen, I.A. Banerjee, R, Djalali, L. Yu, H. Matsui, Langmuir, 20, 8409 (2004).
  24. “Biological Bottom-Up Assembly of Antibody Nanotubes on Patterned Antigen Arrays”, N. Nuraje, I.A. Banerjee, R.I. MacCuspie, L. Yu and H. Matsui, J. Am. Chem. Soc., 126, 8088 (2004).(the Most-Accessed Article in 2007, http://pubs.acs.org/journals/jacsat/promo/most/most_accessed/index.html)
  25. “Doughnut-Shaped Peptide Nano-Assemblies and Their Applications as Nanoreactors”, R. Djalali, J. Samson, H. Matsui, J. Am. Chem. Soc., 126, 7935 (2004).
  26.  “Size-Controlled Ni Nanocrystal Growth on Peptide Nanotubes and Their Magnetic Properties”, L. Yu, I.A. Banerjee, M. Shima, K. Rajan, H. Matsui, Adv. Mater., 16, 709 (2004).
  27. “Incorporation of Sequenced Peptides on Nanotubes for Pt Coating: Smart Control of Nucleation and Morphology via Activation of Metal Binding Sites on Amino Acids”, L. Yu, I.A. Banerjee, H. Matsui, J. Mater. Chem., 14, 739 (2004).
  28. “Direct Growth of Shape-Controlled Nanocrystals on Nanotubes via Biological Recognition”, L. Yu, I.A. Banerjee, H. Matsui, J. Am. Chem. Soc., 125, 14837 (2003).
  29. “Cu Nanocrystal Growth on Peptide Nanotubes via Biomineralization: Size Control of Cu Nanocrystals by Tuning Peptide Conformation”, I.A. Banerjee, L. Yu, H. Matsui, Proc. Natl. Acad. Sci. USA, 100, 14678 (2003).
  30. “Application of Host - Guest Chemistry in Nanotube-Based Device Fabrication: Photochemically Controlled Immobilization of Azobenzene Nanotubes on Patterned alpha-CD Monolayer/Au Substrates via Molecular Recognition”, I.A. Banerjee, L. Yu, H. Matsui, J. Am. Chem. Soc., 125, 9542 (2003).
  31. “Nanocrystal Growth on Nanotube Controlled by Conformations and Charges of Sequenced Peptide Templates”, R. Djalali, Y-F, Chen, H. Matsui, J. Am. Chem. Soc., 125, 5873 (2003). 
  32. “Location-Specific Biological Functionalization on Nanotubes" Attachment of Proteins at the Ends of Nanotubes Using Au Nanocrystal Masks”, I.A. Banerjee, L. Yu, , H. Matsui, Nano Lett., 3, 283 (2003). 
  33. “Au Nanowire Fabrication From Sequenced Histidine-Rich Peptide”, R.Djalali, Y-F, Chen, H. Matsui, J. Am. Chem. Soc., 124, 13660 (2002).
  34. “Size-controlled peptide nanotube fabrication using polycarbonate membranes as templates”, P. Porrata, E. Goun, H. Matsui, Chem. Mater., 14, 4378 (2002).
  35. “Organic Nanotube-Bridge Fabrication by Controlling Molecular Self-Assembly Processes between Spherical and Tubular Formations”, H. Matsui, C. Holtman, NanoLett., 2, 887 (2002).  
  36. “Protein Tubule Immobilization on Self-Assembled Monolayers on Au Substrates”, H. Matsui, P. Porrata, G.E. Douberly, Jr., NanoLett,1, 461 (2001).
  37. "Metalloporphyrin Nanotube Fabrication Using Peptide nanotubes as Templates", H. Matsui and R. MacCuspie, NanoLett., 1, 671 (2001)
  38. "Fabrication of Protein Tubules: Immobilization of Proteins on Peptide Tubules", G.E. Douberly Jr., S. Pan, D. Walters, H. Matsui, J. Phys. Chem. B. 105, 7612 (2001).
  39. "Organization of Peptide Nanotubes into Macroscopic Bundles", H. Matsui and G.E. Douberly Jr., J. Phys. Chem. B., 17, 7918 (2001).  "Controlled Immobilization of Peptide Nanotube-Templated Metallic Wires on Au Surfaces ", H. Matsui, B. Gologan, S. Pan and G.E. Douberly Jr., Eur. Phys. J. D. 16 , 403 (2001).
  40. "Fabrication of Nanocrystal Tubule Using Peptide Nanotube Template and Its Application as Signal-Enhancing Nano-Cuvette", H. Matsui, S. Pan and G.E. Douberly Jr., J. Phys. Chem. B., 105, 1683 (2001).    
  41. "BolaamphiphileNanotube-Templated Metallic Wires", H. Matsui, S. Pan, B. Gologan, and S. Jonas, J. Phys. Chem. B., 104, 9576 (2000)."Crystalline GlycylglycineBolaamphiphile Tubules and their pH - Sensitive Structural Transformation", H. Matsui and B. Gologan, J. Phys. Chem. B., 104, 3383 (2000).              
  42. "Nanoconstruction of Microspheres and Microcapsules Using Proton-Induced Phase Transitions: Molecular Self-Recognition by DiamideDiacids in Water", O. Phanstiel IV, R.J. Lachicotte, D. Torres, M. Richardson, H. Matsui, H. Schaffer, F. Adar, J. Liu, and D. Seconi, Chem. Mater., 13, 264 (2001).
  43. "Mechanism of DicarboxamideMicrosphere Self-Assembly Probed by In situ Raman Microscopy and Raman Imaging", H. Matsui, B. Gologan, H. Schaffer, F. Adar, D. Seconi, and O. PhanstielLangmuir, 16, 3148 (2000).  

 

B. Review Articles

  1. “Room temperature material synthesis using biomimetic peptide nanoreactors and their controlled assemblies on surfaces”, CMC Publisher, Tokyo, “Bio/Nano process”, Chapter 28, (2008).
  2. “Peptide-Based Nanotubes and Their Applications in Bionanotechnology”, X. Gao, H. Matsui, Adv. Mater., 17, 2037 (2005).
  3. “Applications of biological nanotubes to device fabrications and material syntheses”, OyoButsuri, Appl. Phys. Japan, 74, 1576-1582 (2005).
  4. “Bionanotechnology: Device fabrication using natural and synthetic peptides”, H. Matsui, in Bio-Industry, CMC Publisher, Tokyo, 22, 27-32 (2005).
  5. “Protein Nanotubes as Building Blocks for Nanotechnology”, H. Matsui, in Dekker Encyclopedia of Nanoscience and Nanotechnology, J.M. Schwarz (Ed), Marcel Dekker, Inc., New York, v.4, 3065-3077 (2004).
  6. “Peptide Nanotubes”, H. Matsui, in Encyclopedia of Nanoscience and Nanotechnology, H.S. Nelwa (Ed), American  Scientific Publishers, Stevenson Ranch, CA, v.8, 445-455 (2004).
  7. “Applications of Synthetic Peptides in Nanomaterials”, H.  Matsui, in Bio-Venture, Yodosha Publisher, Tokyo, 4, 17-21 (2004).
  8. “Self-Assembled Peptide Nanotube: Assembling Mechanism and Fabrications”, H. Matsui, Recent Research Developments in Physical Chemistry, 5th Edition, Transworld Research Network, 351-370 (2003).

 

 C. Other Publications

  1. “Investigation of Resonantly Selected Raman Spectra of Intermediates in Organic Pyrolysis Reactions”, H. Matsui, N. Kobko, J.J. Dannenberg, S.H. Jonas, R. Viswanathan, J. Raman. Spec. 33, 443 (2002).
  2. "Distribution of DNA in Cationic Liposome Complexes Probed by Raman Microscopy", H. Matsui and S. Pan, Langmuir, 17, 571 (2001).
  3. "Resonance Raman Spectroscopic Investigation of the Mechanism and Kinetics of Nylon 6,6 Degradation", H. Matsui, C.A.Schehr, J.J. Valentini and J.N. Weber, Polymer, 42, 5625 (2001)
  4. "Conformation Change of Poly(dG-dC)oPoly(dG-dC) in Cationic Polyamine Liposome Complexes: Effect of Charge Density and Flexibility of Amine Chains in Head Groups", H. Matsui and S. Pan, J. Phys. Chem. B., 104, 8871 (2000).
  5. "Resonance Raman Studies of Photoinduced Decomposition of Nylon 6,6: Product Identification and Mechanistic Determination", H. Matsui, S.M. Arrivo, J.N. Weber, and J.J. Valentini, Macromolecules, 33, 5655 (2000).
  6. "FTIR and Abinitio Studies of Nitrosoketene via Pyrolysis of IsonitrosoMeldrum's Acid", H. Matsui, N. Katagiri, T. Sugihara and C. Kaneko, J. Phys. Chem. A, 101, 3936 (1997).

 Current Group Members:

Postdoctral Fellows: Ramin Djalali (Ph.D., Johannes Gutenberg-University, Mainz; Present Address, Unilever Co.), Ipista Banerjee (Ph.D., University of Conneticut; Present Address, Fordham Univ, Assistant Professor) , Gao Xuyen (Ph.D., the Chinese Academy of Science, Present Address, Univ. Illinois), Christopher Spedaliere (Ph.D. Univ. Delaware, Present Address, Univ. Nebraska), Anne Runge (Ph.D., Univ. Arizona), Sang-Yup Lee (Ph.D., Purdue Univ.)

Graduate Students: Yung-fou Chen, Lingtao Yu, Stewart Hung, Precila Porrata, Robert MacCuspie, Germaine Muniz ,Witold Chawarski, Nurxat Nuraje , Lillian Yuan, Hanying Bai, Christophe Pejoux

Undergraduate Students: Amit Haboosheh, Andy Chen

High School Students (Solomon Schechter): Elahd Bar-Shai, Amitai Cohen-Halberstam