The Department of Macromolecular Science comprises three core laboratories and one cooperative laboratory, with each laboratory comprising several research groups. Click on a laboratory name for more details.
Macromolecular Synthesis & Reactions
1. Syntheses of well-defined polymers with various
characteristic properties by living cationic polymerization.
2. Syntheses of advanced stimuli-responsive block copolymers.
3. Investigation of polymerization mechanism and design of novel living polymerization.
Home Page: http://www.chem.sci.osaka-u.ac.jp/lab/aoshima/e_index.html
Concept of macromolecular design and living polymerization
for syntheses of well-designed stimuli-responsive polymers
1. Development of new organometallic polymerization
catalysts and their application to synthesis of functional
2. Functional macromolecular complexes composed of organometallic units
3. Investigation of the reactivity controlling mechanism in the active center of metalloenzyme using model complexes having simple ligands and/or short peptides.
4. Synthesis of non-natural amino acid polymers for higher order structure formation and expression of novel functions.
5. Sequence and function analyses of proteins and protein complexes using novel metal complex sequencing reagents.
Home Page: http://www.chem.sci.osaka-u.ac.jp/lab/onitsuka/e
Macromolecular Structure, Properties, and Functions
2. Nonlinear rheology and rheo-optics of polymer solids.
3. Molecular motions of hyper-branched polymers.
4. Structure and molecular motions of supramolecules.
5. Hydration and molecular motions of water-soluble polymers
6. Structure and dynamics of polymer composites.
Soft matter stands for soft materials including polymers, liquid crystals, suspensions, and self-assembling molecules which form a large mesoscopic structure much larger than atoms. Soft matters are “soft” and therefore they can easily respond to external fields like strain fields, flow fields, electric fields and so on, and sometimes show drastic structural changes. We have been studying their unique physicochemical properties, particularly nonlinear responses under strong external fields, in addition to their fruitful equilibrium properties and dynamics. Our research is focused on molecular interpretation of rheological phenomena of polymers and micelles as a model system of soft matter.
Home Page: http://www.chem.sci.osaka-u.ac.jp/lab/inoue/index_Eng.html
Akihito HASHIDZUME (Professor), Yuri KAMON (Assistant Professor)
(1) We synthesize precise macromolecules with well-defined chemical structures because these precise macromolecules are critical for deeper understanding of macromolecularity.
(2) We strive to understand macromolecularity utilizing the precise macromolecules.
(3) We challenge existing boundaries to creation of high-performance macromolecules comparative to biological macromolecules using the precise macromolecules.
Home Page: http://www.chem.sci.osaka-u.ac.jp/lab/hashidzume/index_eng.html
In this laboratory, we develop novel materials through hybridization of bio-related macromolecules such as monoclonal antibodies with artificial/synthetic small molecules. We construct functionalized catalytic and energy conversion systems based on specific molecular recognition of biomacromolecules and selective assembly of bio/synthetic molecules.
Home Page: http://www.chem.sci.osaka-u.ac.jp/lab/yamaguchi/english/
1.Rotational mechanism of the bacterial flagellar motor.
2. Self-assembly mechanism of the bacterial flagellar motor.
3. Structural and functional studies on bacterial protein secretion systems.
4. Structural and functional studies on environmental sensing units of bacteria.
5. Study on the structure of polymer complex with small molecule and its formation mechanism.
Home Page: http://www.chem.sci.osaka-u.ac.jp/lab/imada/en/
The flagellar type III export apparatus and F/V-type ATPases share a common architecture.
1. Syntheses of novel associating polymers with strong attractive interactions, like amphiphilic polyelectrolytes, random copolymers bearing carboxyl and amide (or amino) groups, etc.
2. Establishment of methods for characterizing polymer conformation in aggregates, self-associating structure, and interaction among polymer aggregates, by using light scattering, fluorescence, NMR, size-exclusion chromatography, viscosity, ultracentrifuge, and so on.
3. Interpretation of various properties of associating polymer solutions, like viscosity, liquid crystallinity, circular dichroism, reaction kinetics, and interaction with functional molecules, in terms of self-associating structure and intermolecular or inter-aggregate interaction.
Home Page: http://www.chem.sci.osaka-u.ac.jp/lab/sato/index-e.html
Informative Polymer Science (Institute for Protein Research)
2. Analysis of structural stability and dynamics of protein molecules.
3. Analysis of structural stability and the mechanism of formation of amyloid fibrils.
Protein folding is a process in which an extended polypeptide chain acquires a unique folded conformation with biological activity. However, the exact molecular mechanism remains unknown. Clarifying the mechanism of protein folding is essential to improve our understanding of the structure and function of proteins. It is also important to design engineered proteins with improved functions.
Moreover, protein folding plays important roles in many biological phenomena. For an example, the deposition of amyloid fibrils has been suggested to play a central role in over 20 degenerative disorders including Alzheimer’s and prion diseases. Because the amyloid fibril deposition is often caused by misfolding of an originally functional protein, these diseases are called “folding disease”. In order to establish therapeutic treatments, clarifying the molecular mechanism of folding diseases is essential.We are studying the conformational stability of proteins, molecular basis of folding reaction, and structures and formation of amyloid fibrils. These studies are performed by using various physicochemical methods (NMR, CD, IR, calorimetry, ultracentrifugation and single molecule observation with fluorescence microscopy) with recombinant proteins expressed by using E.coli and yeast.
Home Page: http://www.protein.osaka-u.ac.jp/physical/index.html
An image of amyloid fibrils of amyloid-β peptide obtained
using total internal reflection fluorescence microscopy.
2. Crystal structure analyses of dynein motor
3. High resolution structural analysis of rat liver vault
Three-dimensional protein structure brings us a deeper insight into the biological function. X-ray crystallography is the best method to determine atomic coordinates of protein molecules. The main aim of our group is the X-ray structure determination of the biological macromolecular assemblies including membrane protein complexes, in order to elucidate the molecular mechanism of the highly organized biological processes at atomic level.
Home Page: http://www.protein.osaka-u.ac.jp/crystallography/EngHP/
Crystal Structure of the dynein motor domain
2. Developing a new crystallographic techniques for structure determination of biological macromolecular assemblies.
3. Structural studies of biological macromolecules and biological macromolecular assemblies.
4. Structural studies on proteins working in brain and nervous system.
Macromolecule assemblies, consisting of proteins, nucleic acids, and other substances, play key roles in all living system. Our laboratory works on structure determination of biological macromolecular assemblies using X-ray diffraction technique. Development of tools for X-ray crystallography of biological macromolecular assemblies, including the synchrotron radiation beamline at SPring-8, is also one of our main works.
Home Page: http://www.protein.osaka-u.ac.jp/rcsfp/supracryst/index.html
Department for the Administration of Safety and Hygiene
2. Development of the photo-switching functional molecules.
3. Development of detection methods for environmental chemicals.
4. Construction of education system for realization of safety concious culture in the university.
5. Research and analyses of university accidents in the world.
This laboratory belongs to the department for the administration of safety and hygiene, whose mission is managing safety and hygiene of all people constituting the university. The research in this laboratory aims to contribute to the safety of wide area in science and technology. At present, our research projects focus on development of new functional molecules such as low barrier ion conductive polymers for the safety of Li ion batteries, photo-switchable hydrogen bonds for environmental chemistry, etc. In addition, our laboratory proposes safe methods and techniques for conducting research and experiments through investigation and analyses of university accidents in the world.
Home Page: http://www.osaka-u.ac.jp/jp/facilities/anzen/kankyou/index.html