KANAZAWA, Japan, April 7, 2020 /PRNewswire/ -- 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.
- Prof. Zerial's accomplishments in cellular and molecular
biology and research on EEA1 "motivated this study".
- Prof. 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.
- Dr. 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
- T. 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
- N. 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
- T. 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
- M. 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
- K. 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
- T. 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
- T. 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/research/researchers/toshio-ando/
Further general information
About the Human Frontier Science Program
2020 awards
for Research Grants
https://www.hfsp.org/awardees/newly-awarded
About WPI nanoLSI Kanazawa University
Hiroe Yoneda
Vice Director of Public Affairs
WPI Nano Life Science Institute (WPI-NanoLSI)
Kanazawa University
Kakuma-machi, Kanazawa 920-1192, Japan
Email: nanolsi-office@adm.kanazawa-u.ac.jp
Tel: +81(76)234-4550
About Nano Life Science Institute (WPI-NanoLSI)
https://nanolsi.kanazawa-u.ac.jp/en/
Nano Life Science Institute (NanoLSI), Kanazawa University is a
research center established in 2017 as part of the World Premier
International Research Center Initiative of the Ministry of
Education, Culture, Sports, Science and Technology. The objective
of this initiative is to form world-tier research centers. NanoLSI
combines the foremost knowledge of bio-scanning probe microscopy to
establish 'nano-endoscopic techniques' to directly image, analyze,
and manipulate biomolecules for insights into mechanisms governing
life phenomena such as diseases.
About Kanazawa University
http://www.kanazawa-u.ac.jp/e/
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.
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