Prof. Toshio Ando and colleagues have been awarded the prestigious Human Frontier Science Program (HFSP) Research Grant
Toshio Ando of the WPI Nano Life Science Institute, Kanazawa University, Electra Gizeli (Principal Applicant, Institute of Molecular Biology and Biotechnology, Foundation for Research and Technology, Greece), Marino Zerial (MPI of Molecular Cell Biology and Genetics, Germany), and Andrew J. Spakowitz (Stanford University, USA) have been awarded a prestigious research grant from the Human Frontier Science Program (HFSP). The research grant is an award of 450,000 USD per year for a period of three years for the collaborative team. The award is for the group’s proposal for multidisciplinary research entitled, “Self-organization and biomechanical properties of the endosomal membrane”.
Toshio Ando is internationally recognized for the development and invention of the in-liquid high-speed atomic force microscope (HS-AFM) for visualizing the dynamics of protein molecules in liquid environments [1-6]. The publication of his seminal paper on HS-AFM in 2008 led Ando and his colleagues to develop derivatives of this technology including non-invasive high-speed scanning ion-conductance microscopy (HS-SICM). “It is a great honor for me to receive this HFSP grant in the worldwide competition,” says Professor Ando.
Comments from the HFSP highlighted the strengths of the team and multidisciplinary nature of the proposal, stating: “This is a very strong team of investigators. Each is highly accomplished in their field and brings unique expertise.”
Roles of the members of the team:
- Team leader Professor Gizeli’s expertise in acoustic measurements to determine the dynamics of EEA1 structural changes.
- Zerial’s accomplishments in cellular and molecular biology and research on EEA1 “motivated this study”.
- Ando’s unique high speed atomic force microscopy instrumentation that enables direct visualization of the structure and dynamics of protein molecules in liquids to measure EEA1 conformational changes.
- Spankowitz’s expertise in multi-scale modeling to develop a model of EEA1 brush behavior.
The Human Frontier Science Program (HFSP) promotes international collaborative basic research on “the elucidation of the sophisticated and complex mechanisms of living organisms”. The programs are implemented by the International Human Frontier Science Program Organization (HFSPO) that is based in Strasburg and receives financial support from the governments or research councils of the European Union, Australia, Canada, France, Germany, India, Italy, Japan, Republic of Korea, New Zealand, Norway, Singapore, Switzerland, United Kingdom, and USA.
Selection of references on research published by Professor Ando on high speed AFM
- Ando, T. Uchihashi, and T. Fukuma, “High-speed atomic force microscopy for nano-visualization of dynamic biomolecular processes,” Prog. Surf. Sci. 83, 337–437, (2008).
DOI: 10.1016/j.progsurf.2008.09.001
- Kodera, D. Yamamoto, R. Ishikawa, and T. Ando, “Video imaging of walking myosin V by high-speed atomic force microscopy”, Nature 468, 72–76 (2010).
DOI: 10.1038/nature09450
- Ando, N. Kodera, D. Maruyama, E. Takai, K. Saito, and A. Toda, “A High-speed atomic force microscope for studying biological macromolecules, Proc. Natl. Acad. Sci. USA98, 12468–12472 (2001).
DOI: 10.1073/pnas.211400898
- Shibata, H. Yamashita, T. Uchihashi, H. Kandori, and T. Ando, “High-speed atomic force microscopy shows dynamic molecular processes in photo-activated bacteriorhodopsin”, Nat. Nanotechnol. 5, 208–212 (2010).
DOI: 10.1038/nnano.2010.7
- Igarashi, T. Uchihashi, A. Koivula, M. Wada, S. Kimura, T. Okamoto, M. Penttilä, T. Ando, and M. Samejima, “Traffic jams reduce hydrolytic efficiency of cellulase on cellulose surface”, Science 333, 1279–1282 (2011).
DOI: 10.1126/science.1208386
- Uchihashi, R. Iino, T. Ando, and H. Noji, “High-speed atomic force microscopy reveals rotary catalysis of rotorless F1-ATPase, Science 333, 755–758 (2011).
DOI: 10.1126/science.1205510 - Uchihashi, Y. Watanabe, T. Yamasaki, H. Watanabe, T. Maruno, K. Ishii, S. Uchiyama, C. Song, K. Murata, R. Iino, and T. Ando, “Dynamic structural states of ClpB involved in its disaggregation function”, Nat. Commun. 9, 2147 (12 pp) (2018).
DOI: 10.1038/s41467-018-04587-w
Prof. Toshio Ando
https://nanolsi.kanazawa-u.ac.jp/en/researcher/18483/
Further general information
About the Human Frontier Science Program
2020 awards for Research Grants
https://www.hfsp.org/awardees/newly-awarded
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As the leading comprehensive university on the Sea of Japan coast, Kanazawa University has contributed greatly to higher education and academic research in Japan since it was founded in 1949. The University has three colleges and 17 schools offering courses in subjects that include medicine, computer engineering, and humanities.
The University is located on the coast of the Sea of Japan in Kanazawa – a city rich in history and culture. The city of Kanazawa has a highly respected intellectual profile since the time of the fiefdom (1598-1867). Kanazawa University is divided into two main campuses: Kakuma and Takaramachi for its approximately 10,200 students including 600 from overseas.
Professor Toshio Ando the inventor of high speed in-liquid atomic force microscopy (HS-AFM) for direct visualization of proteins in action.
Fig. 1: Walking myosin
Fig. 2 Molecular Chaperone ClpB
Fig. 3 GroEL-GroES Interaction