AFOB Newsletter

vol.22
October 15, 2023

My Lab

Prof. Yoichi Kumada

Si-Yu Li, Ph.D

Associate Professor Yoichi Kumada,
Faculty of Molecular Chemistry and Engineering,
Kyoto Institute of Technology, Kyoto, Japan.
Co-Principle Investigator (Co-PI), Group Leader, Laboratory of Chemical and Biochemical Engineering Laboratory
Expert in Bio-separation and Bio-recognition engineering / Antibody Engineering / Affinity Chromatography





Greetings AFOB community,

It is a great pleasure to introduce our team on the AFOB community. The Biochemical Engineering Laboratory (Kumada Group) in the Department of Molecular Chemistry at Kyoto Institute of Technology is conducting engineering research to maximize the potential of biomolecules, including antibodies, using original and unique approaches, and to contribute to the establishment of a healthy and safe society. Our research group focuses on development of next generation of biomolecular recognition reagents for more precise and selective affinity separation of biomolecules that has been considerably important in the fields of industrial biopharmaceutical production as well as sensitive immunological tests. We have particularly studied immobilization of antibodies and their fragments onto the surfaces of a variety of materials utilizing our original 쏮aterials-Binding Peptides (MBPs). MBPs that are preferentially adsorbed on the target surfaces with strong binding affinity can be identified and isolated from our original protein/peptide resources and can be introduced at the terminal regions of target proteins such as single-chain variable fragments (scFvs) and single-domain antibodies (VHHs).

The MBP-fused scFv antibodies that we are developing are much smaller in molecular size than the conventional antibodies and can be densely immobilized on the surface of materials by strong binding affinity of MBPs. This adhesion region, namely MBPs can physically link the antibody itself to the surface of the substrate material. This technology is very unique and has many advantages and possibilities. In order to achieve the perfect immobilization of antibodies, it is also necessary to take on the great challenges of protein/peptide engineering, surface chemistry and materials science. Combination of our original technologies with the other distinguished technologies will create economical and precise biorecognition surface that will be highly useful for the purpose described above.

Our research group very welcomes graduate students and researchers to achieve the goals together, and we are looking forward to exchanging ideas, enhancing technologies and contributing health science with you in near future.

References
  • Y. Kumada*, R. Tanibata, K. Yamamoto, H. Noguchi, A. Angelini, J. Horiuchi, Development and characterization of a latex turbidimetric immunoassay using rabbit anti-CRP single-chain Fv antibodies, Journal of Immunological Methods, in press
  • Y. Kumada*, H. M. Rakotondravao, Y. Hasegawa, Y. Iwashita, H. Okura, S. Uchimura, J. Horiuchi, Strategies for selection and identification of rabbit single-chain Fv antibodies as ligand in affinity chromatography, Journal of Bioscience and Bioengineering, 134, 233-239 (2022)
  • H. M. Rakotondravao, R. Takahashi, T. Takai, Y. Sakoda, J. Horiuchi, Y. Kumada*, Control of accessible surface area and height equivalent to a theoretical plate by grafted dextran during anion-exchange chromatography of therapeutic proteins, Journal of Chemical Engineering of Japan, 55, 267-274 (2022)
  • J. Blazeck, C. S. Karamitros, K. Ford, C. Somody, A. Qerqez, K. Murray, N. T. Burkholder, N. Marshall, A. Sivakumar, W. C. Lu, B. Tan, C. Lamb, Y. Tanno, M. Y. Siddiqui, N. Ashoura, S. Coma, X. M. Z., K. McGovern, Y. Kumada, Y. J. Zhang, M. Manfredi, K. A. Johnson, S. D섲rcy, E. Stone, G. Georgiou, Bypassing evolutionary dead-ends and switching the rate-limiting step of a human immunotherapeutic enzyme, Nature Catalysis, 5, 952-967 (2022)
  • Y. Kumada*, Y. Hasegawa, J. Horiuchi, Efficient and robust isolation of rabbit scFv antibodies using antigen-coupled multilamellar vesicles, Journal of Bioscience and Bioengineering, 131, 299-304 (2021)
  • Y. Kumada*, Y. Miyamura, R. Tanibata, K. Takahashi, S. Ogasawara, F. Gondaira, J. Horiuchi, Design and site-directed immobilization of single-chain Fv antibody to polystyrene latex beads via material-binding peptides and application to latex turbidimetric assay, Journal of Bioscience and Bioengineering, 131, 84-89 (2021)
  • Y. Kumada*, Y. Miyamura, R. Tanibata, K. Takahashi, S. Ogasawara, F. Gondaira, J. Horiuchi, Design and site-directed immobilization of single-chain Fv antibody to polystyrene latex beads via material-binding peptides and application to latex turbidimetric assay, Journal of Bioscience and Bioengineering, 131, 84-89 (2021)




  • Laboratory members