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Hiroshi Matsui, Ph.D.

Professor - Bionanotechnology

 Hiroshi

Contact Information:

office 1319N (tel 212-650-3918), lab 1317N/1318N (tel 212-650-3916), dept fax 212-772-5332, email hmatsui@hunter.cuny.edu, group webpage Matsui Group Homepage

Education:

B.S. Sophia University, Japan, M.S. Stanford University, Ph.D. Purdue University, Postdoc Columbia University

Research Summary: 

Matsui’s group is working in the fields of Nanotechnology and Biotechnology and the integration of these two areas (i.e., Bionanotechnology) is producing creative sciences with high technology impacts. Matsui’s research interests consist of; 1. 3D Assembly of Nanomaterials using peptide framework (target: solar cells, metamaterials, electronics, optics), 2. Reconfigurable/programable self-assembly system, 3. Development of cancer cell sensing silicon chips 4. Origin of life discovering catalytic peptides (i.e., enzyme-mimic) through virus evolution.

The ability to control self-assembly of complex 2D and 3D architectures from functional building blocks could allow further development of complex device configurations. By mimicking natural systems, genetically engineered peptides with a variety of functional building blocks such as metal NPs can be applied to design new materials with the specificity of assembled structure, the robustness of assembly, and the versatility of the superstructure. Here, we present three types of large-scale (µm3 ~ mm3) biomimetic 2D and 3D assemblies using nanoscale collagen peptides as building blocks. The first example is to mimic bone tissues for the production of free-standing flexible collagen films. In this case, biotylated collagen peptides are assembled into films with streptavidin-functionalized QDs, which are used as molecular recognition-based cross-linking agents between biomolecular film domains to provide structural reinforcement and flexibility. The second example is to mimic S-layer proteins on bacteria and we assemble microcapsules from collagen peptides stable even in extreme pH or high temperature when the peptides are assembled on oil-in water droplets and the ends of peptides are capped/cross-linked by peptide-binding proteins. The third example is to assemble 3D reconfigurable superstructure crystals from collagen peptides in the large-scale with high yield. In this strategy, biotylated collagen peptides and ligand-functionalized nanoparticle hubs are self-assembled into 3D microcrystals in controlled structures and NP density with the precise nanoscale interparticle distance. This simple, rapid fabrication protocol produces high yields of 3D materials in controlled shapes, promising ease and flexibility in manufacturing future functional devices.  The reconfigurability of the 3D directed assembly was also demonstrated by modifying peptides with genetic engineering. We discovered that the conformation change of peptide building blocks induced by pH could trigger the disassembly of the hybrid NP-peptide cube and undergo the reassembly into different shapes. One of innovative applications for reconfigurable assembly is to develop autonomous metal-organic-framework (MOF) motors driven by re-assembly of peptides from inside to outside of MOF.  

Another part of Matsui'research is to develop biosensor chips for detecting cancer cells. One of the best strategies to halt cancer’s progress is the development of new diagnostic tools that allow one to detect the disease in an early stage. It would be desirable to develop simple and robust cancer detection systems without using unreliable biomarkers for a variety of tumor grades regardless of its origin in early stages. The development of non-invasive screening device for cancers with high specificity and selectivity enables more frequent monitoring of the early stage disease development, progress, recovery, and recurrence of cancers. Here we developed a new cancer detection platform incorporating electric cancer cell sensors on silicon chips. This sensing platform was designed to distinguish cells in different sizes and shapes by measuring their characteristic impedance signals on polysilicon microelectrodes. Due to the softness of cancer cells as compared to normal cells, cancer cells were observed to swell three times more than normal cells under hyposmotic pressure. By using this sensor chip and protocol, cancer cells can be distinguished from normal cells electronically without biomarkers; as strong hyposmotic stress is applied to cells, only cancer cells increase impedance signals due to the distinguished mechanical property. For example, we have examined six different cancer cell lines from prostate, kidney, ovarian, and breast, and all of these cancer cells were observed to expand their size about 35 – 50 % under osmotic pressure and their swellings could be detected sensitively and selectively by the robust impedance measurements of the sensor chip on the order of 10 cells/mL in less than 30 minutes even in contaminated samples. Recently, we improved the protocol to detect cancer cells in urine samples. Finally, the aggressive breast cancer cells could be distinguished from less aggressive ones by measuring impedance values of the samples, opening the possibility that circulating tumor cells (CTC), cancer stem cell (CSC), or metastatic cancer cells may be detected by this technique.

The third part is for the discovery of new catalytic peptides through virus evolution. The amide bond is fundamental to life. It acts as the strong chemical linkage between amino acids as they combine to form proteins. As such, its high stability against spontaneous hydrolysis at physiological conditions is paramount, with an estimated half-life of 600 years for internal peptide bonds. Nonetheless, several key processes in the biological world involve the breaking (hydrolysis) and reforming (condensation) of the amide bond. Through evolution, nature has generated a variety of amidolytic catalysts in the form of enzymes that enable both effective hydrolysis and condensation of amide bonds. Despite a series of impressive advances in the last 30 years, most notably using catalytic antibodies, our ability to mimic this behavior through the de novo design and discovery of amidolytic catalysts that operate under physiological conditions and can hydrolyse internal peptide bonds has been unsuccessful. our strategy of catalytic capture via condensation-driven gelation, combined with phage display was successful in the identification of four different dodeca peptides which specifically catalyze the formation/cleavage of amide bonds. These peptides can spontaneously fold into   minimal catalytic triads. The result reported here would break through the prescriptive concept that catalytic oligopeptides cannot acquire the substrate-specificity because of the lack of complicated 3D structures that enzymes posses. This concept is also applicable to discover catalytic peptides to grow a variety of semiconductor nanomaterials at room temperature. To demonstrate the proof-of-concept, we examined to find catalytic peptides for room-temperature growth of ZnO nanocrystal by this approach. The combinatory phage display library identified the small number of peptide sequences for the ZnO growth and one of them, ZP-1 peptide, demonstrated the strong catalytic activity for the room temperature growth.

Selected Publications

“New Autonomous Motors of Metal-Organic Framework (MOF) Powered by Reorganization of Self-Assembled Peptides at interfaces”, Y. Ikezoe, G. Washino, T. Uemura, S. Kitagawa, H. Matsui, Nature Mater., 11, 1081 (2012).

“Genetically engineered protein nanowires: Unique features in site-specific functionalization and multi-dimensional self-assembly”, Y. Maeda, H. Matsui, Soft Matter, 8, 7533-7544 (2012).

 “Biomimetic assembly of proteins into microcapsules on oil-in-water droplets with structural reinforcement via biomolecular recognition-based cross-linking of surface peptides”, Y. Maeda, Z. Wei, H. Matsui, Small, 8, 1341-1344 (2012).

“Genetically engineered protein nanowires: Unique features in site-specific functionalization and multi-dimensional self-assembly”, Y. Maeda, H. Matsui, Soft Matter, 8, 7533 (2012).

“Biomimetic Fabrication of Strong Freestanding Genetically-Engineered Collagen Peptide Films Reinforced by Quantum Dot Joints”, Z. Wei, Y. Maeda, H. Matsui, Soft Matter, 8, 6871 (2012).

 “One-Pot Crystalline ZnO Nanorod Growth in Mineralizing Peptide Gels”, L. Anjia, Z. Wei, H. Matsui, RSC Adv., 2, 5516 (2012).

“Effects of Divalent Metals on Nanoscopic Fiber Formation and Small Molecule Recognition of Helical Proteins”, S.K. Gunasekar, L. Anjia, H. Matsui, J.K. Montclare, Adv. Func. Mater. 22, 2154 (2012).

 “Discovery of Catalytic Peptides for Inorganic Nanocrystal Synthesis by a Combinatorial Phage Display Approach”, Z. Wei, Y. Maeda, H. Matsui, Angew. Chem. Intl. Ed., 50, 10585, (2011). (selected as a hot paper in 2011).

 “Direct Enzyme Patterning with Microcontact Printing and the Growth of ZnO Nanoparticles on the Catalytic Templates at Room Temperature”, K.I. Fabijanic, R. Perez-Castillejos , H. Matsui, J. Mater. Chem., 21, 16877, (2011). (invited article in a special issue on ‘Self-Organisation of Nanoparticles’)

“Assemblies of functional peptides and their applications in building blocks for biosensors”, R. de la Rica, C. Pejoux, H. Matsui, Adv. Func. Mater. 21, 1018 (2011).

“3D Self-Assembly of Peptide Nanowires into Micron-Sized Crystalline Cubes with Nanoparticle Joints”, P. Kaur, Y. Maeda, A.C. Mutter, T. Matsunaga, Y. Xu, and H. Matsui, Angew. Chem. Intl. Ed., 49, 8375-8378 (2010). (selected as a highlight paper in 2010)

“Applications of peptide and protein-based materials in bionanotechnology”, R. de la Rica, H. Matsui, Chem. Soc. Rev., 39, 3499 - 3509 (2010)

“Bio-inspired Target-specific Crystallization on Peptide Nanotubes for Ultra-Sensitive Pb Ion Detection”, R. de la Rica, E. Mendoza, H. Matsui, Small, 6, 1753-1756 (2010).

"Peptide Nanotube Biochips for Label-Free Multiplexed Pathogen Detection”, R. de la Rica, C. Pejoux, C. Fernandez-Sanchez, A. Baldi, and H. Matsui, Small, 6, 1092 (2010).

“Biomimetic crystallization nanolithography; Simultaneous nanopatterning and crystallization”, R. de la Rica, K.I. Fabijanic, A. Baldi, and H. Matsui, Angew. Chem. Intl. Ed., 49, 1447 (2010). (featured in NanoWerk News in 2010, http://www.nanowerk.com/spotlight/spotid=15020.php).

“PbSe nanocrystal growth as nanocubes and nanorods on peptide nanotubes via different directed-assembly pathways”, M. Shi, W. Su, and H. Matsui, Nanoscale, 2, 2373-2376 (2010).

"Label-free cancer cell detection with impedimetric transducers”, R. de la Rica, S, Thompson, A. Baldi, C. Fernández-Sánchez, C.M. Drain, and H. Matsui, Anal. Chem., 81, 10167 (2009). (featured as research news in the National Cancer Institute in 2009, http://physics.cancer.gov/news/2009/dec/po_news_e.asp.

“Biomimetic conformation-specific assembly of proteins at artificial binding sites nano-patterned on silicon”, R. de la Rica, H. Matsui, J. Am. Chem. Soc., 131, 14180 (2009).

“­­­Selective detection of live pathogens via surface-confined electric field perturbation on interdigitated silicon transducer”, R. de la Rica, A. Baldi, C. Fernández-Sánchez, and H. Matsui, Anal. Chem., 81, 3830 (2009).

“Biomineralization Nanolithography: Combination of Bottom-Up and Top-Down Fabrications to Grow Arrays of Monodisperse Au Nanoparticles along Peptide Lines on Substrates”, N. Nuraje, S. Mohammed, L. Yang, and H. Matsui, Angew. Chem. Intl. Ed., 48, 2546 (2009). (selected as a hot paper in 2009).

“Low temperature synthesis of ZnO nanowire by using a genetically modified collagen-like triple helix as a catalytic template”, H. Bai, F. Xu, L. Anjia, and H. Matsui, Soft Matter, 5, 966 (2009).

“Label-Free Pathogen Detection with Peptide Nanotube-Assembled Sensor Chips”, R. de la Rica, E. Mendoza, L.M. Lechuga, and H. Matsui, Angew. Chem. Intl. Ed., 47, 9752 (2008).

“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).

“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).

“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).

“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).

"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).

“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 (published on line as a hot paper) (2007).

“Biomimetic and Aggregation-Driven Crystallization Route for Room-Temperature Material Synthesis: Growth of beta-Ga2O3 Nanoparticles Using Peptide Assemblies as Nanoreactors”, S.Y. Lee, X. Gao, H. Matsui, J. Am. Chem. Soc., 129, 2954 (2007).