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3rd

NanoLSI Symposium
at UBC in Vancouver- Supramolecular Chemistry and Nanoprobes in Life Sciences -August 8, 2019
Thursday9 : 00 am – 6 : 00 pm

Department of Chemistry, The University of British Columbia- Symposium: Chemistry (CHEM) - D300
- Banquet: The Gallery Patio and Lounge, UBC Campus

PROGRAMME
Speaker

9:00

Chair

Opening remarks

9 : 10

Takeshi Fukuma

Visualizing Subnanometer Structures atNanobio-Interfaces by 2D & 3D-AFM

9 : 30Sarah A. Burke

Chemistry atom-by-atom: Probing reactivity ofsurface-bound metal-terpyridine sites by STM and AFM

10: 00Noriyuki Kodera

Video imaging of bio-molecule in action by
high-speed atomic force microscopy(NanoLSI)(The University of British Columbia)(NanoLSI)

10: 20Hitoshi Asakawa(NanoLSI)

Hitoshi Asakawa(NanoLSI)

Hitoshi Asakawa(NanoLSI)

Break

10: 35

Yasufumi Takahashi

Live cell functional imaging using scanning probe
microscopy

10: 55

Hitoshi Asakawa

Molecular-scale distribution and dynamics of host-guest
complexes investigated by FM-AFM and HS-AFM

Katsuhiro Maeda

11: 15

Shigehisa Akine

Design of new host molecules with open/close functions

Katsuhiro Maeda

11: 35Ramesh Jasti(NanoLSI)(NanoLSI)(NanoLSI)(University of Oregon)

12: 05

Carbon Nanohoops as New Biological Imaging Tools

Katsuhiro Maeda(NanoLSI)(NanoLSI)(NanoLSI)

Katsuhiro Maeda(NanoLSI)

Lunch break

13: 30

Satoshi Arai

Visualization and Control of Cellular Activities​byThermodynamic Engineering

Mark MacLachlan

13: 50Russ Algar

Not Everybody Dyes: Leveraging Quantum Dots and Other
Luminescent Nanomaterials for New Opportunities in Bioanalysis

Mark MacLachlan

14: 20David M. Perrin

One-step 18F-labeling for PET Oncology(NanoLSI)(The University of British Columbia)(The University of British Columbia)

14: 50(The University of British
Columbia/NanoLSI)(The University of British
Columbia/NanoLSI)Mark MacLachlan(The University of British
Columbia/NanoLSI)

Break

15: 05

Ratmir Derda

15: 35

Amy Szuchmacher Blum
(McGill University)

Plasmonics with Viruses

16: 05

Kunio Matsumoto

Macrocyclic Peptides Targeting HGF-MET(University of Alberta)(NanoLSI)

16: 25

4

Title

Genetically-Encoded Technologies for Discovery ofInstructive Biomaterials

Russ Algar(The University of British
Columbia)

Russ Algar(The University of British
Columbia)

Russ Algar(The University of British
Columbia)Break

16: 40Satoru Okuda

Versatile modeling of three-dimensional multi-cellular dynamics: in-silico
and in-vitro combined approach to self-organizing morphogenesis

Kunio Matsumoto

17: 00

Satoshi Toda

Synthetic tissue formation: Programming
multicellular self-organization

Kunio Matsumoto

17: 20Wendell Lim

Learning to program cellular machines

Kunio Matsumoto(NanoLSI)(University of California, San Francisco/NanoLSI)(University of California, San Francisco)

17: 50

Closing remarks

18: 30Banquet(NanoLSI)(NanoLSI)(NanoLSI)ORAL PRESENTATION
P6

Takeshi Fukuma

NanoLSI

P8

Sarah A. Burke

The University of British Columbia

P10

Noriyuki Kodera

P12

Yasufumi Takahashi

P14

Hitoshi Asakawa

NanoLSI

P16

Shigehisa Akine

NanoLSI

P18

Ramesh Jasti

University of Oregon

P20

Satoshi Arai

NanoLSI

P22

Russ Algar

P24

David M. Perrin

P26

Ratmir Derda

P28

Amy Szuchmacher Blum

P30

Kunio Matsumoto

P32

Satoru Okuda

NanoLSI

P34

Satoshi Toda

University of California, San Francisco/NanoLSI

P36

Wendell Lim

University of California, San Francisco

NanoLSI

NanoLSIThe University of British Columbia

The University of British Columbia

University of Alberta

McGill University

NanoLSI5

Takeshi Fukuma
Nano Life Science Institute (WPI-NanoLSI), Kanazawa University

Contact : fukuma@staff.kanazawa-u.ac.jp

Research Interests
Atomic Force Microscopy, Nanotechnology, Solid-Liquid Interfaces, Nanobio-science

Education
2003

Doctor of Engineering, Department of Electronic Science and Engineering, Kyoto University

Professional Career
2001 - 2005

Research Fellow, Kyoto University

2005 - 2007

Senior Scientist, Physics Department, Trinity College Dublin (Ireland)2007 - 2012

Associate Professor, Frontier Science Organization, Kanazawa University

2012 - present2017 - present

Professor, Division of Electronic Eng. and Computer Sci., Professor, Kanazawa University
Director/Professor, Nano Life Science Institute (WPI-NanoLSI), Kanazawa University

Scientific Activities
1999 - 2003
2003 - present

Instrumentation and applications of atomic-resolution ultrahigh vacuum AFM.
Instrumentation and applications of atomic-resolution liquid-environment AFM.

Honors
2011
2017
2018

The Young Scientists’ Prize, The Commendation for Science and Technology by the MEXT
Hokkoku Bunka Award, Hokkoku Shinbun
15th JSPS Prize, Japan Society for the Promotion of Science

Publications
T. Fukuma, R. Garcia, “Atomic- and Molecular-Resolution Mapping of Solid−Liquid Interfaces by 3D Atomic Force Microscopy”, ACS Nano, 12 (2018)

1. 11785-11797.

2. K. Miyata, J. Tracey, K. Miyazawa, V. Haapasilta, P. Spijker, Y. Kawagoe, A. S. Foster, K. Tsukamoto, T. Fukuma, Nano Lett., 17 (2017) 4083-4089.
K. Honbo, S. Ogata, T. Kitagawa, T. Okamoto, N. Kobayashi, I. Sugimoto, S. Shima, A. Fukunaga, C. Takatoh, T. Fukuma, ACS Nano,10 (2016)

3. 2575-2583.
6

Visualizing Subnanometer Structures atNanobio-Interfaces by 2D & 3D-AFM
Takeshi Fukuma
Nano Life Science Institute (WPI-NanoLSI), Kanazawa University

At a solid-liquid interface, water molecules interact with a surface to present non-uniform three-dimensional(3D) distribution referred to as hydration structures. In addition, atoms and molecules constituting the surface are notnecessarily static but dynamically fluctuating or diffusing to induce various interfacial phenomena. Consequently, asolid-liquid interface is not two-dimensional but has a three-dimensional extent. However, such 3D fluctuating
structures are very difficult to image, which has limited our understanding on various interfacial phenomena in biology,
physical chemistry, electrochemistry, tribology, mineralogy and environmental sciences. To overcome this problem, we
have been working on the development and applications of 3D atomic force microscopy (3D-AFM) [1]. In thistechnique, AFM tip is scanned in a 3D interfacial space and the force applied to the tip during the scan is recorded to
produce a 3D force image. During the tip scan, the tip interacts
with surrounding water and other flexible molecules so that theobtained force map represents their time-averaged distribution. So
far, this method is mostly used for visualizing hydration structures
on various minerals such as mica, calcite, fluorite and graphite.
However, it is also shown that it can be used for visualizing
hydration structures of softer materials such as biologicalmolecules (e.g., bRs, GroELs and DNAs). One of thesemeasurements, imaging of a lipid/water interface [2], suggests thatthe obtained force image reflects not only the hydration structures
but also the 3D distribution of flexible molecular chains. Thisimplies that 3D-AFM may allow us to visualize various 3D
structures as long as the tip can penetrate into the subsurface area
without causing irreversible damages. To explore this possibility,
we have been working on visualization of various interfacial
structures with different level of complexity and inhomogeneity.

Fig. 1: 3D-AFM imaging of nanobio interfaces.

References[ 1 ] T. Fukuma, Y. Ueda, S. Yoshioka, H. Asakawa, “Atomic-Scale Distribution of Water Molecules at the Mica-Water
Interface Visualized by Three-Dimensional Scanning Force Microscopy”, Phys. Rev. Lett., 104 (2010) 016101.
[ 2 ] H. Asakawa, S. Yoshioka, K. Nishimura, T. Fukuma, “Spatial Distribution of Lipid Headgroups and Water Molecules
at Membrane/Water Interfaces Visualized by Three-Dimensional Scanning Force Microscopy”, ACS Nano, 6 (2012)
9013-9020.
[ 3 ] T. Fukuma, R. Garcia, “Atomic- and Molecular-Resolution Mapping of Solid−Liquid Interfaces by 3D Atomic ForceMicroscopy”, ACS Nano 12 (2018) 11785−11797.

7

Sarah A. Burke
Dept. of Physics & Astronomy, and Dept. of Chemistry
Quantum Matter Institute
University of British Columbia
Contact : saburke@phas.ubc.ca

Research Interests
Electronic structure, surface chemistry, light-matter interactions, scanning probe microscopy

Education
2002
2005
2009

BSc(Hons.) Physics, Dalhousie University, Halifax, NS
MSc Physics, McGill University, Montreal, QC
PhD Physics, McGill University, Montreal, QC

Professional Career2009 - 2010

NSERC Postdoctoral Fellow, UC Berkeley

2010 - 2017

Assistant Professor, University of British Columbia

2017 - present

Associate Professor, University of British Columbia

Honors2010 - 2020

Canada Research Chair (tier 2) in Nanoscience

Publications
Agustin Schiffrin, Martina Capsoni, Gelareh Farahi, Chen-Guang Wang, Cornelius Krull, Marina Castelli, Tanya S. Roussy, Katherine A. Cochrane,

1. Yuefeng Yin, Nikhil Medhekar, Adam Q. Shaw, Wei Ji*, and Sarah A. Burke*, “Designing optoelectronic properties by on-surface synthesis: formationand electronic structure of an iron-terpyridine macromolecular complex”, ACS Nano, 12(7) (2018); 6545-6553

K. A. Cochrane, T. S. Roussy, B.-K. Yuan, G. Tom, E. Mårsell, S. A. Burke*, “Molecularly Resolved Electronic Landscapes of Differing Acceptor-Donor

2. Geometries”, Journal of Physical Chemistry C, 122(15) (2018); 8437-8444

K. A. Cochrane, A. Schiffrin, T. Roussy, M. Capsoni, S. A. Burke*, “Pronounced polarization-induced energy level shifts at boundaries of organic

3. semiconductor nanostructures” Nature Communications 6 (2015): 8312

8

Chemistry atom-by-atom: Probing reactivity ofsurface-bound metal-terpyridine sites by STM and AFM
Sarah A. Burke
Department of Physics & Astronomy, Department of Chemistry, and the Quantum Matter Institute,
University of British Columbia, Vancouver, BC, Canada

Heterogeneous catalysts play a vital role in numerous industrial chemical processes, yet their complexity – involving interfaces
and a distribution of reactive sites – can hamper mechanistic understanding and efforts towards rational design.
Surface-bound molecular catalysts offer the potential to create identical reactive sites – especially by exploiting highfidelity self-assembly methods – bringing the benefits of molecular design from homogeneous catalysts toheterogeneous systems. Scanning tunneling microscopy (STM), spectroscopy (STS) and non-contact atomic force
microscopy (ncAFM) provide unique atomistic views of surface structures and the frontier molecular orbitals that giverise to reactivity.


I will describe our recent work investigating the reactivity of self-assembled surface-bound Fe-terpyridine (tpy) species[1,2] with small-molecule gaseous reagents using STM, STS, and ncAFM at low temperatures (4-40K) in ultrahighvacuum. STM and ncAFM images indicate that both CO and ethylene react with the undercoordinated Fe-tpy sites via asurface-bound intermediate step prior to forming a chemical bond with the Fe site. STS of the nascent and bonded
species shows a distinctive signature for each reactant, indicative of changes in the frontier orbitals responsible forfurther reactivity. Statistical analyses show that subsequent annealing steps up to 40K lead to ensemble progression
through these reaction stages and towards higher-order structures, indicating that reactivity can be induced at
low-temperature through minimal heating, and revealing the reaction pathway. The ability to probe individualcomponents of the distribution while also building ensemble data allows us to identify and characterize intermediate
reaction steps, providing detailed reaction pathway information about this novel well-defined surface-bound reactive site.

References[ 1 ] Agustin Schiffrin, Martina Capsoni, Gelareh Farahi, Chen-Guang Wang, Cornelius Krull, Marina Castelli,
Tanya S. Roussy, Katherine A. Cochrane, Yuefeng Yin, Nikhil Medhekar, Adam Q. Shaw, Wei Ji*,
and Sarah A. Burke*, “Designing optoelectronic properties by on-surface synthesis: formation and electronic
structure of an iron-terpyridine macromolecular complex”, ACS Nano, 2018, 12(7) 6545-6553[ 2 ] Cornelius Krull, Marina Castelli, Prokop Hapala, Dhaneesh Kumar, Anton Tadich, Martina Capsoni,Mark T. Edmonds, Jack Hellerstedt, Sarah A. Burke, Pavel Jelinek and Agustin Schiffrin* “Iron-based trinuclear
metal-organic nanostructures on a surface with local charge accumulation”, Nature Commun, 2018, 9, 3211

9

Noriyuki Kodera
Nano Life Science Institute (WPI-NanoLSI), Kanazawa University

Contact : nkodera@staff.kanazawa-u.ac.jp

Research Interests
Biophysics, molecular motors, cytoskeletons, atomic force microscopy

Education
Mar. 2001

B. Sci., Dept. of Phys, Fac. of Sci., Kanazawa Univ.

Mar. 2003

M. Sci., Div. of Math. & Phys. Sci., Grad. Sch. Nat. Sci. & Tech., Kanazawa Univ.

S e p . 2005

Ph.D., Div. of Basic Sci., Grad. Sch. Nat. Sci. & Tech., Kanazawa Univ.

Professional Career2005 - 2010

Research Fellow (DC2 & PD), JSPS and Postdoctoral Fellow, CREST, JST2010 - 2018

Assistant Professor & Associate Professor, Bio-AFM Frontier Research Center,
Institute of Science and Engineering, Kanazawa University

2013 - 20172018 - present

PRESTO Researcher, JST
Professor, Nano Life Science Institute (WPI-NanoLSI), Kanazawa University

Scientific Activities
2000 - 2008

Development of high-speed atomic force microscopy (HS-AFM)

2008 - present

Biological application studies using HS-AFM and improvement of HS-AFM

Honors
2012

Young Researcher’s Nanoprobe Technology Prize (JSPS Nanoprobe Technology 167)

2013

Prize for Science and Technology (Development Category), The Commendation for Scienceand Technology by the Minister of Education, Culture, Sports, Science and Technology

2017

JSPS Prize

Publications
Terahara N, Kodera N, Uchihashi T, Ando T, Namba K, Minamino T, “Na+-induced structural transition of MotPS for stator assembly of the Bacillus

1. flagellar motor”, Science Advances 3, eaao4119 (2017).

Ngo KX, Kodera N, Katayama E, Ando T, Uyeda TQ, “Cofilin-induced unidirectional cooperative conformational changes in actin filaments revealed

2. by high-speed atomic force microscopy”, eLife 4, 04806 (2015).

3. Kodera N, Yamamoto D, Ishikawa R, Ando T, “Video imaging of walking myosin V by high-speed atomic force microscopy”, Nature 468, 72-76 (2010).
10Video imaging of bio-molecule in action by
high-speed atomic force microscopy
Noriyuki Kodera
Nano Life Science Institute (WPI-NanoLSI), Kanazawa University

We have been developing a high-speed atomic force microscopy (HS-AFM) that can directly observe biologicalmolecules in action at nanometer spatial and sub-second temporal resolution (Fig.1a) [1]. The unique performance of
HS-AFM has been demonstrated by direct observations of proteins, protein-protein complexes (Fig.1b), protein-nucleic
acid complexes (Fig.1d), and cellular surface [2]. Importantly, HS-AFM can even resolve thin and flexible features of
intrinsically disordered regions (IDRs), single polypeptide chains with height of ~0.5 nm, in a protein that could not beanalyzed by any techniques at single molecule level (Fig.1c). In some cases, dynamic structural transitions in IDRs
between ordered- and disordered-conformations can be directly visualized [3-5].
In this presentation, we will overview the principle and current performance of HS-AFM, and then show recent
activities on improvement of scanning performance (super high-speed Z-scanner and high-speed amplitude detector
for cantilever oscillation) and functional extensions (PDMS-based concave-convex substrate, high-speed scanner with amanipulator, and HS-AFM system combined with patch clump) of HS-AFM.

Fig.1 (a) Principle of HS-AFM (left), photograph of HS-AFM (upper right) and its
merits (lower right). (b-d) Gallery of HS-AFM movies. (b) Myosin-V walking along
actin filament. (c) Wiggling motion of an IDR of FACT protein. (d) Targeted
dsDNA digestion by CRISPR-Cas9.

References[ 1 ] T. Ando, T. Uchihashi, and N. Kodera, Anuu. Rev. Biophys., 2013, 42, 393-414.
[ 2 ] T. Ando, T. Uchihashi, and S. Scheuring, Chem. Rev., 2014, 114, 3120-3188.
[ 3 ] M. Hashimoto, N. Kodera, Y. Tsunaka, M. Oda, M. Tanimoto, T. Ando, K. Morikawa, and S. Tate, Biophys. J., 2013,
104, 2222-2234.
[ 4 ] N. Kodera, K. Uchida, T. Ando, and S. Aizawa, J. Mol. Biol., 2015, 427, 406-414.
[ 5 ] N. Terahara, N. Kodera, T. Uchihashi, T. Ando, K. Namba, and T Minamino, Sci. Adv., 2017, 3, eaao4119.

11

Yasufumi Takahashi
Nano Life Science Institute (WPI-NanoLSI), Kanazawa University

Contact : yasufumi@se.kanazawa-u.ac.jp

Research Interests
Live cell functional imaging, chemical sensing, scanning probe microscopy

Education
2004
2006
2009

B.Sc. in Engineering, Tohoku University
M.Sc. in Environmental science, Tohoku University
Ph.D. in Environmental science, Tohoku University

Professional Career
2011 - 2013

Research Assistant, Tohoku University

2013 - 2015

Assistant Professor, Tohoku University

2015 - present

Associate Professor, Kanazawa University

Scientific Activities
2004 - 2009

Development of high resolution scanning electrochemical microscopy for live cell imaging

2009 - 2011
2011 - present

Development of SECM-SICM for live cell imaging
Development of nanoscale chemical sensor for live cell metabolite detection

Honors20162017

Young Scientists’ Prize of the Commendation for Science and Technology by the Minister of
Science and Technology
Bioindustry Award

Publications
1. Zhou, Y. S.; Saito, M.; Miyamoto, T.; Novak, P.; Shevchuk, A. I.; Korchev, Y. E.; Fukuma, T.; Takahashi, Y., Anal Chem 2018, 90 (4), 2891-2895.
Zhang, Y.; Clausmeyer, J.; Babakinejad, B.; Cordoba, A. L.; Ali, T.; Shevchuk, A.; Takahashi, Y.; Novak, P.; Edwards, C.; Lab, M.; Gopal, S.; Chiappini,

2. C.; Anand, U.; Magnani, L.; Coombes, R. C.; Gorelik, J.; Matsue, T.; Schuhmann, W.; Klenerman, D.; Sviderskaya, E. V.; Korchev, Y., Acs Nano 2016, 10(3), 3214-3221.

3. Nashimoto, Y.; Takahashi, Y.; Zhou, Y. S.; Ito, H.; Ida, H.; Ino, K.; Matsue, T.; Shiku, H., Acs Nano 2016, 10 (7), 6915-6922.
12

Live cell functional imaging using
scanning probe microscopy
Yasufumi Takahashi
Nano Life Science Institute (WPI-NanoLSI), Kanazawa University

Dynamic visualization of extracellular chemical concentration profile around the live cell is important forunderstanding the cell metabolic state, cell-cell interaction, and relationship between chemical concentration and cellfunction. However, still it is not established chemical sensor for detect the chemical around the single cell.
Scanning ion conductance microscopy (SICM) uses a less than 50 nm radius nanopipette for detecting ion
current and is an effective tool for non-contact live cell nanoscale topography imaging, local chemical delivery, andcytosol collection (Fig.1). We have developed miniaturized electrochemical sensor and mounted the sensor on SICM
probe to achieve chemical (oxygen, catecholamine, H2O2) and topographical simultaneous imaging.1,2 To improve theelectrochemical imaging resolution and sensitivity, we developed nanoscale electrode3 and chemical sensing field-effective
transist (FET) probe4. These probes are effective to visualize nanoscale chemical distribution and μM level of the chemicals
detection.
The local cytosol collection is also important technique to reveal the localization of mRNAs at a single cell level.
We have developed a hybrid system of SICM and electrochemical syringe to collect the localized mRNA of single living
cells. The system uses double-barrel glassn a n o p i p e t t e a s a p ro b e . 5 T h i s s y s t e m
successfully detected local differences in Actb
mRNA expression levels in single mouse
fibroblast cells.
High speed SICM is effective to visualize
the cell surface dynamic change.6 To reduce
the scanning time, we selected next scanningarea at the specific region by using previous
obtained topography information (Patent
2016-188803). By using this scanning mode,
we visualized the volume change of neurites,
transport of cargo molecule transport, andthe structure change of growth cone.
Figure 1 Schematic illustration of SICM and hippocampus neuron topography image.

References[ 1 ] Takahashi, Y.; et al. J. Am. Chem. Soc. 2010, 132 (29), 10118-10126.
[ 2 ] Takahashi, Y.; et al. Angew. Chem. Int. Ed. 2011, 50 (41), 9638-9642.
[ 3 ] Takahashi, Y.; et al. Proc. Natl. Acad. Sci. U. S. A. 2012, 109 (29), 11540-11545.
[ 4 ] Zhang, Y. et al. Acs Nano 2016, 10 (3), 3214-21.
[ 5 ] Nashimoto, Y.; Takahashi, Y. et al. Acs Nano 2016, 10 (7), 6915-22.
[ 6 ] Ida, H.; et al. Anal. Chem. 89, 6015-6020, (2017).

13

Hitoshi Asakawa
Nanomaterials Research Institute, Kanazawa University, Japan

Contact : hi_asa@staff.kanazawa-u.ac.jp

Research Interests
Atomic force microscopy in liquid
Direct measurement of intermolecular interactions at the single molecular level
Self-assembly of chemical and biological molecules at solid/liquid interfaces

Education
2007

PhD in Biological Functions Engineering, Kyushu Institute of Technology, Japan

Professional Career2008 - 2010

Postdoctoral Fellow, Frontier Science Organization, Kanazawa University, Japan

2010 - 2016

Assistant Professor, Bio-AFM Frontier Research Center, Kanazawa University, Japan

2016 - present

Associate Professor, Division of Material Chemistry, Kanazawa University, Japan2017 - present

Associate Professor, Nano Life Science Institute (WPI-NanoLSI), Kanazawa University, Japan2018 - present

Associate Professor, Nanomaterials Research Institute (NanoMaRi), Kanazawa University, Japan

Honors2013
2019

Nanoprobe technology young scientist award from No. 167 committee of Japan society forthe promotion of science (JSPS)
The young scientist prize from the ministry of education, culture, sports, science and technology (MEXT)

Publications
1. Asakawa, H.; Holmström, E.; Foster, S. A.; Kamimura, S.; Ohno, T.; Fukuma, T., J. Phys. Chem. C, 2018, 122, 24085-24093.
2. Asakawa, H.; Inada, N.; Hirata, K.; Matsui, S.; Igarashi, T.; Oku, N.; Yoshikawa, N.; Fukuma. T., Nanotechnology, 2017, 28, 455603.
3. Asakawa, H.; Yoshioka, S.; Nishimura, K.; Fukuma T., ACS Nano, 2012, 6, 9013-9020.

14

Molecular-scale distribution anddynamics of host-guest complexes
investigated by FM-AFM and HS-AFM
Hitoshi Asakawa
Nanomaterials Research Institute, Kanazawa University, JapanThe reversible association-disassociation process is one of the critical molecular systems in biology and chemistry.
For example, environmentally responsible materials are often developed based on the reversible association propertiesof host-guest complexes. To investigate the properties of complex formations, several analytical methods have been
well established with spectroscopies and calorimetry such as XRD, NMR, and ITC. However, direct observation of hostguest complexes is very challenging, even with such established methods. Hence, the spatial distribution of host-guest
complexes and their dynamics remain unclear. Frequency-modulation atomic force microscopy (FM-AFM) has proven to
be a powerful technique for investigating surface structures with subnanometer resolution in liquid [1]. Besides, recent
advances in high-speed AFM (HS-AFM) have enabled us to determine molecular dynamics with a frame rate of over 10
frames/s [2]. Here, we present a molecular-scale investigation on the distribution of host-guest complexes and theirdynamics in liquid using both FM-AFM and HS-AFM.
A macrocyclic host structure referred to as pillar[5]arene (P[5]A) and n-alkanes with anionic headgroups were used asa host structure and guest molecules, respectively. P[5]A is known to capture n-alkane moieties of guest molecules by
CH/π interactions with high selectivity [3]. Recently, we reported that cationic P[5]A molecules form self-assembled
monolayers with a hexagonal molecular arrangement on mica [4]. In this study, structural changes by the formation of
host-guest complexes were investigated by FM-AFM. The FM-AFM images show that subnanometer-scale particle-like
contrasts become clearer with increasing the concentration of anionic guest molecules. We found that the association
constant of P[5]A-guest complexes is able to be determined from the obtained FM-AFM images. The association
constant was a reasonable value even compared with the expected from other analytical methods. In addition,
dynamic reversibility of P[5]A-guest complex formation was also visualized by FM-AFM and HS-AFM imaging. The
results suggested that the AFM techniques should contribute to the molecular-scale understanding of associationdisassociation process not only host-guest complex but also various molecular systems in chemistry and biology.

References[ 1 ] Fukuma, T., Rev. Sci. Instrum., 2009, 80, 023707.
[ 2 ] Shibata, M.; Yamashita, H.; Uchihashi, T.; Kandori, H.; Ando, T., Nat. Nanotech., 2010, 5, 208-212.
[ 3 ] Ogoshi, T.; Yamagishi, T., Chem. Commun., 2014, 50, 4776-4787.
[ 4 ] Ogoshi, T.; Takashima, S.; Inada, N.; Asakawa, H.; Fukuma, T.; et al., Commun. Chem., 2018, 1, 29.

15

Shigehisa Akine
Nano Life Science Institute (WPI-NanoLSI), Kanazawa University

Contact : Tel +81-76-264-5701 E-Mail akine@se.kanazawa-u.ac.jp

Research Interests
1. Coordination-based functional systems for molecular recognition and chirality control
2. Dynamic structural conversion of multi-metal complexes

Education
1991 - 1995
1995 - 1997
1997 - 2000

B. S. Department of Chemistry, Faculty of Science, The University of Tokyo
M. S. Department of Chemistry, Graduate School of Science, The University of Tokyo
PhD Department of Chemistry, Graduate School of Science, The University of Tokyo

Professional Career2000 - 2004

Research Associate, Department of Chemistry, University of Tsukuba

2004 - 2008

Assistant Professor, Graduate School of Pure and Applied Sciences, University of Tsukuba

2008 - 20132013 - 2017

Associate Professor, Faculty of Pure and Applied Sciences, University of Tsukuba

2017 - present

Professor, Nano Life Science Institute (WPI-NanoLSI), Kanazawa University

Professor, Graduate School of Natural Science and Technology, Kanazawa University

Honors
2011
2011

DIC Award in Synthetic Organic Chemistry JapanHGCS Japan Award of Excellence

Publications“Ligand Exchange Strategy for Tuning of Helicity Inversion Speeds of Dynamic Helical Tri(saloph) Metallocryptands”

1. Sakata, Y.; Chiba S.; Miyashita, M.; Nabeshima, T.; Akine, S. Chem. Eur. J. 2019, 25, 2962–2966.
“A Closed Metallomolecular Cage that can Open its Aperture by Disulfide Exchange”

2. Akine, S.; Miyashita, M.; Nabeshima, T. Chem. Eur. J. 2019, 25, 1432–1435.

“Anion-capped metallohost allows extremely slow guest uptake and on-demand acceleration of guest exchange”

3. Sakata, Y.; Murata, C.; Akine, S. Nat. Commun. 2017, 8, 16005.

“A Metallo-molecular Cage That Can Close the Apertures with Coordination Bonds”

4. Akine, S.; Miyashita, M.; Nabeshima, T. J. Am. Chem. Soc. 2017, 139, 4631–4634.
16

Design of new host molecules with open/close functions
Shigehisa Akine
Nano Life Science Institute (WPI-NanoLSI), Kanazawa University
Graduate School of Natural Science and Technology, Kanazawa University

Macrocyclic compounds and molecular cages are known to act as a good host molecule. Usual host molecules easilyand quickly take up a guest species in the cavity, but some molecular cages can permanently confine the guest species
in the cavity. This confinement effect depends on the guest size compared with the cage structures, because only theguest species that are smaller than the cage portal can enter and exit the cavity. If we introduce a cap function into thehost compounds, we can switch the guest confinement effect; the guest is confined in the cavity when the cap isclosed, while the guest freely enters and exits when the cap is open. In order to achieve this open/close function, we
designed two new molecular scaffolds based on oligo(salen)–metal structures. [1] In this lecture, guest recognition
control behavior of the macrocyclic and cage-like oligo(salen) structures will be presented.
1. Cage-like metallocryptand that can close the aperture.[2] A tricobalt(III) metallocryptand [L1Co3(hda)3](OTf)3, whichhas 1,6-hexanediamine (hda) ligands at the apertures of the molecular cage, was synthesized. This complex selectively
recognized Cs+, but it took more than 50 h for the complete conversion to the Cs+ complex. The uptake rate was morethan 2000 times slower than that of the open cage analogue. The closed-cage structure with diamine ligands efficiently
slowed down the guest uptake.
2. Anion-capped macrocyclic metallohost.[3] A macrocyclic dicobalt(III) metallohost [L2Co2(MeNH2)4] (OTf)2 recognizedvarious cations (Na+, K+, Rb+, Ca2+, La3+) to give the inclusion complexes, in which the binding site was capped with two
triflate anions. The guest uptake became significantly slow due to the capping effect so that we could obtain kineticallytrapped state where a disfavored guest was taken up prior to a favored guest. Based on the fact that the capping effectdepends on the type of anions, we achieved an on-demand guest exchange triggered by replacing the anion caps
starting from the kinetically trapped state.

References[ 1 ] S. Akine, J. Inclusion Phenom., 2012, 72, 25; S. Akine and T. Nabeshima, Dalton Trans., 2009, 10395.
[ 2 ] S. Akine, M. Miyashita, T. Nabeshima, J. Am. Chem. Soc., 2017, 139, 4631.
[ 3 ] Y. Sakata, C. Murata, S. Akine, Nat. Commun., 2017, 8, 16005.

17

Ramesh Jasti
University of Oregon

Contact : rjasti@uoregon.edu

Research Interests
The organic synthesis of precision carbon nanomaterials with unique properties and applications.

Education
1998
2006

B.S. with Honors at the University of North Carolina, Chapel Hill
PhD at the University of California, Irvine

Professional Career2009 - 20142014 - present

Boston University
University of Oregon

Scientific Activities
2009 - 20142014 - 2019

Assistant Professor of Chemistry, Boston University
Associate Professor of Chemistry and Biochemistry, University of Oregon

HonorsNSF Career Award, Alfred P. Sloan Fellowship, Camille Dreyfus Teacher-Scholar Award

Publications
Jasti, R.; Bhattacharjee, J.; Neaton, J. B.; Bertozzi, C. R. "The Synthesis, Characterization, and Theory of [9]-, [12]-, and [18]Cycloparaphenylene:

1. Carbon Nanohoop Structures." J. Am. Chem. Soc. 2008, 130, 17646-17647.

Sisto, T. J.; Golder, M. R.; Hirst, E. S.; Jasti, R. "Selective Synthesis of Strained [7]Cycloparaphenylene: An Orange-Emitting Fluorophore."

2. J. Am. Chem. Soc. 2011, 133, 15800-15802.

Evans, P. J.; Darzi, E. R.; Jasti, R. "Efficient Room-Temperature Synthesis of a Highly Strained Carbon Nanohoop Fragment of Buckminsterfullerene."

3. Nat. Chem. 2014, 6, 404-408.

18

Carbon Nanohoops as New Biological Imaging Tools
Ramesh Jasti
University of Oregon

In their simplest form, nanohoops can be thought of as short slices of carbon nanotubes. In this lecture, I will describe
my research group’s impetus for developing synthetic methods to prepare a wide range of these types of structures.
I will also detail the unique size-dependent optical properties of these molecules, which are direct manifestations of theunusual radially oriented π-systems. Finally, I will share our most recent results to elaborate this new class of nanoscalebuilding blocks into materials useful for biological imaging.[1,2,3]References[ 1 ] Darzi, E. R.; Jasti, R. "The Dynamic Size-Dependent Properties of [5]-[12] Cycloparaphenylenes."
Chem. Soc. Rev. 2015, 44, 6401-6410.

[ 2 ] White, B. M.; Zhao, Y.; Kawashima, T. E.; Branchaud, B. P.; Pluth, M. D.; Jasti, R. "Expanding the Chemical Space of
Biocompatible Fluorophores: Nanohoops in Cells." ACS Cent. Sci. 2018, 4, 1173-1178.

[ 3 ] Lovell, T. C.; Colwell, C. E.; Zakharov, L. N.; Jasti, R. "Symmetry Breaking and the Turn-On Fluorescence of Small,
Highly Strained Carbon Nanohoops." Chem. Sci. 2019, 10, 3786.

19

Satoshi Arai
Nano Life Science Institute (WPI-NanoLSI), Kanazawa University

Contact : satoshi.arai.chem@gmail.com

Research Interests
My research background comprises expertizes such as chemical biology, polymer chemistry, and biophysics. Our greathope is to visualize and manipulate cellular events in all living organism from viewpoint of thermodynamics. To achievethis, we generated fluorescent sensors to light up cellular elements such as temperature and ATP. Recent years, we
further focused on the development of “thermodynamic engineering technology”, where temperature could be controlled at nano/microscale quantitatively.

Education
2004
2007

M.S., Polymer Chemistry, Waseda University
PhD (D. Eng.), Polymer Chemistry, Waseda University

Professional Career2007 - 20092009 - 2010
2 011 - 2012
2 012 - 2016
2 016 - 2019
July. 2019 - present

Research Associate, Department of Life Science and Medical Bioscience, Waseda University
Postdoctoral Fellow, Cooperative Bio Science Research Institute, Waseda University
Research Fellow, National University of Singapore (prof. Chang Young-Tae Lab)
Senior Research Fellow, WASEDA Bioscience Research Institute in Singapore
Assistant Professor, WASEDA Bioscience Research Institute in Singapore, Waseda University
Associate Professor (Tenure-track), Nano Life Science Institute (WPI-NanoLSI), Kanazawa University

Scientific Activities
2015 - present

PRIME Researcher (Japan Agency for Medical Research and Development, AMED)2019 - present

Visiting Researcher (Nanyang Technological University)

Honors2014
2014
2 018 - 2019

The Award for Encouragement of Research in IUMRS-ICA2014
Tanaka Kikinzoku Kogyo, MMS award
JSPS-LEADER (candidate)Publications
RGB-Color Intensiometric Indicators to Visualize Spatiotemporal Dynamics of ATP in Single Cells, S. Arai, R. Kriszt, K. Harada, L-S. Looi, S. Matsuda,

1. D. Wongso, S. Suo, S. Ishiura, Y-H. Tseng, M. Raghunath, T. Ito, T. Tsuboi, T. Kitaguchi, Angew. Chem. Int. Ed., vol.57, pp.10873-10878 (2018).

Gold Nanoshell-Mediated Remote Myotube Activation, A. Marino, S. Arai, Y. Hou, A. Degl'Innocenti, V. Cappello, B. Mazzolai, Y-T. Chang, V. Mattoli, M. Suzuki, G. Ciofani,2. ACS Nano vol.11, pp.2494–2508 (2017). Highlighted at “Gold nanoparticles: A warm-up for muscle cells” Nature Nanotechnology 12. 188 (2017).

A Molecular Fluorescent Probe for Targeted Visualization of Temperature at the Endoplasmic reticulum, S. Arai, S-C. Lee, Z. Duanting, M. Suzuki, Y-T.

3. Chang, Sci. Rep., vol.4, 6701 (2014).
20

Visualization and Control of Cellular Activities​by Thermodynamic Engineering​
Satoshi Arai
Nano Life Science Institute (WPI-NanoLSI), Kanazawa University

Very recently, it was discovered that a certain fish, the opah, generates heat by themselves in order to warm up his
body for predation activities in the deep sea (Wegner et al, 2015). Recent studies also revealed that dinosaur seems
reasonable to be categorized between warm and cold blooded animals (Grady et al, 2014). These findings are likely togive fresh surprises for those who understands generating heat (thermogenesis) to be the unique property in only
mammalians and birds. At the same time, they would teach us how important temperature is as an inherent parameterto drive chemical reactions in all living systems.
Our research is focused on the visualization of an energy flow in living cells, where key elements are temperature andATP. To date, we have developed various fluorescence sensors to visualize intracellular temperature and ATP [1,2].
Recent achievement also includes “Thermodynamic Engineering Technology”, enabling to measure and control
temperature at nano/microscale using photothermal materials and temperature sensing dyes [3]. Using this technology,
we attempted to induce the rapid apoptosis in cancer cells and muscle contraction. In this talk, we are going to share
the tips of these topics and more than welcome for fruitful discussion.

References[ 1 ] RGB-Color Intensiometric Indicators to Visualize Spatiotemporal Dynamics of ATP in Single Cells, S. Arai, R. Kriszt,
K. Harada, L-S. Looi, S. Matsuda, D. Wongso, S. Suo, S. Ishiura, Y-H. Tseng, M. Raghunath, T. Ito, T. Tsuboi, T. Kitaguchi,
Angew. Chem. Int. Ed., 2018, 57, 10873-10878.
[ 2 ] Nanosized Optical Thermometers, Smart Nanoparticles for Biomedicine (ed. by Gianni Ciofani), Elsevier, *S. Arai,
M. Suzuki, 2018, Chapter 14, 199-217.
[ 3 ] Gold Nanoshell-Mediated Remote Myotube Activation, A. Marino, S. Arai, Y. Hou, A. Degl'Innocenti,
V. Cappello, B. Mazzolai, Y-T. Chang, V. Mattoli, M. Suzuki, G. Ciofani, ACS Nano, 2017, 11, 2494–2508.

21

Russ Algar
Department of Chemistry, University of British Columbia, 2036 Main Mall,
Vancouver, V6T 1Z1, Canada.
Contact : algar@chem.ubc.ca

Research Interests
My research group is interested in the development of luminescent materials for applications in bioanalysis andbioimaging, including but not limited to point-of-care diagnostic devices, multiplexed probes, molecular photonic logic,
new materials development, and fundamental studies of photophysics and how nanomaterials interact with biologicalmolecules and systems.

Education
2005
2010

Hon.B.Sc. University of Toronto
Ph.D. University of Toronto

Professional Career2010 - 2012

NSERC Postdoctoral Fellow, Center for Bio/Molecular Science and Engineering,
US Naval Research Laboratory, Washington, DC, USA

2012 - 20182018 - present

Assistant Professor, University of British Columbia
Associate Professor, University of British Columbia

Scientific Activities
2012 - present
2014 - present

Canada Research Chair in Bio/Chemical Sensing

2019 - present

Features panel member, Analytical Chemistry (ACS)Michael Smith Foundation for Health Research Scholar

Honors
2017
2017
2017
2018

Canadian Society for Chemistry (CSC) Fred Beamish Award in Analytical Chemistry
Spectroscopy magazine Emerging Leader in Molecular Spectroscopy
Alfred P. Sloan Foundation Research Fellowship
The Power List 2018: Top 40 Under 40 by The Analytical Scientist magazine

Publications
1. E. Petryayeva, W.R. Algar*, Analyst, 2015, 140, 4037-4045.
2. M. Massey, I.L. Medintz, M.G. Ancona, W.R. Algar*, ACS Sensors, 2017, 2, 1205-1214.
3. M. Massey, H. Kim, E. Conroy, W.R. Algar*, J. Phys. Chem. C, 2017, 121, 13345–13356.
22

Not Everybody Dyes: Leveraging Quantum Dots andOther Luminescent Nanomaterials for
New Opportunities in Bioanalysis
W. Russ Algar
Department of Chemistry, University of British Columbia, Vancouver, BC, Canada.

Fluorescent dyes and proteins are great—except when they’re not. Colloidal semiconductor quantum dots (QDs) are
excellent alternatives for fluorescent dyes—except when they’re not. With the wide and growing variety of luminescentmaterials available, no single material is best-suited to every application [1]. This presentation will overview ourresearch in developing methods of bioanalysis that leverage QDs and other luminescent nanomaterials to achieve
capabilities that are both suited to the nanomaterial and not possible with fluorescent dyes or proteins alone. These
include smartphone-based platforms for biomolecular and cellbased assays [2-4], as well as single-vector multiplexed concentric
FRET probes toward cellular sensing [5-7]. Special attention will be
paid to our ongoing development of multifunctional composites of
QDs and magnetic or plasmonic nanoparticles. The opticalproperties of these composites overcome the deficiencies of asmartphone for fluorescence measurements without requiringsophisticated engineering. With the composite nanoparticles and asimple 3D-printed device, we are able to isolate and count HER2positive cancer cells against a background of HER2-negative cells.
This work is now moving toward barcoded assays for multiplexed
cell detection, cell-surface antigen profiling, and single-analyte
detection on a smartphone. A primary goal of our research is todevelop materials and devices that make molecular medicine moreaccessible, whether at the bedside or in remote or low-resource
settings.

References[ 1 ] W.J. Peveler, W.R. Algar*, ACS Chem. Biol. 2018, 13, 1752-1766.
[ 2 ] E. Petryayeva, W.R. Algar*, Analytical Chemistry 2014, 86, 3195-3202.
[ 3 ] E. Petryayeva, W.R. Algar*, Analyst 2015, 140, 4037-4045.
[ 4 ] E. Petryayeva, W.R. Algar*, Anal. Bioanal. Chem. 2016, 408, 2913-2925.
[ 5 ] M. Wu, W.R. Algar*, Anal. Chem. 2015, 87, 8078-8083.
[ 6 ] M. Massey, H. Kim, E. Conroy, W.R. Algar*, J. Phys. Chem. C 2017, 121, 13345–13356.
[ 7 ] W.R. Algar*, et al., J. Am. Chem. Soc. 2017, 139, 363-372.

23

David M. Perrin
Chemistry Department – University of British Columbia

Contact : dperrin@chem.ubc.ca

Research Interests
Bioorganic Chemistry, Chemical Biology, DNAzymes, PET imaging agents, Peptide natural products

Education
1990
1995

BA Biochemistry UC Berkeley
Ph.D. Biological Chemistry, UCLA

Professional Career
1995 - 2000
2000 - present

Postdoctoral Fellow
Professor, UBC

Publications
A densely modified M2+-Independent DNAzyme capable of efficient all-RNA cleavage and mammalian cell membrane penetration, Yajun Wang, Erkai

1. Liu, Curtis H. Lam, and David M. Perrin* Chemical Science 2018 9: 1813-1821.
18

F-Organotrifluoroborates as Radioprosthetic Groups for PET Imaging: From Design Principles to Preclinical Application, David M. Perrin*,

2. Acc. Chem. Res. 2016 49: 1333-1343.

Synthesis of the death-cap mushroom toxin -Amanitin, Kaveh Matinkhoo, Alla Pryyma, Mihajlo Todorovic, Brian O. Patrick, and David M. Perrin*

3. J. Am Chem. Soc. 2018 140: 6513-6517.

24

One-step 18F-labeling for PET Oncology
David M. Perrin
Chemistry Department, University of British Columbia

The American oncology tracer market will grow annually at >8% to >$8B. Driving this growth are peptides that detectspecific molecular targets whose dysregulation and presence leads to cancer.1 While several PET-useful isotopes exist,
18

F-fluoride is the only isotope with a track-record of FDA clearance and which can be produced at Curie-levels,

on-demand.2 Nevertheless, the challenges for 18F-labeling large molecules are considerable; these include a short half-lifeand the need to work in anhydrous conditions.3 Hence most peptide labelings require 2-4 steps including a preliminary
drying step, various steps related to precursor synthesis, and an HPLC step to remove unreacted peptide in a radiosynthetic
process normally requiring 70-180 min.4 In seeking a water-friendly reaction, we developed several organotrifluoroborates
that can be conjugated to peptides to provide precursors that are 18F-labeled by isotope exchange in a single aqueous
step.5 Because the unlabeled 19F-precursor and 18F-labeled product are chemically inseparable (they differ by only aneutron), a final HPLC step may often be avoided. This allows for an
exceptionally time-efficient radiolabeling method of a single step. We
believe this method will be generalizable to many peptides as we havesuccessfully labeled RGD, bombesin, octreotate, and bradykinin. 6-10
Preclinical animal data with 18 F-RBF 3 -octreotate provide a comparable
profile to that seen with 68 Ga-DOTA-TATE. In pursuit of dual-mode
fluorescent PET tracers, we have conceived of a “radiosynthon” that lets
researchers graft any peptide and a fluorophore of choice to provide tracersthat combine the sensitivity of PET with the brilliance of fluorescence.

References
1 . Tsien, R. Y., Imagining imaging's future. Nat. Cell Biol. 2003, Ss16-Ss21.
2 . Eberl, S.; Eriksson, T.; Svedberg, O.; Norling, J.; Henderson, D.; Lam, P.; Fulham, M., High beam current operation ofa PETtrace (TM) cyclotron for F-18(-) production. Appl. Radiat. Isot. 2012, 70 (6), 922-930.

3 . Cai, L. S.; Lu, S. Y.; Pike, V. W., Chemistry with F-18 fluoride ion. Eur. J. Org. Chem. 2008, (17), 2853-2873.
4 . Chin, F. T.; Shen, B.; Liu, S. L.; Berganos, R. A.; Chang, E.; Mittra, E.; Chen, X. Y.; Gambhir, S. S., First Experience
with Clinical-Grade F-18 FPP(RGD)(2): An Automated Multi-step Radiosynthesis for Clinical PET Studies. Mol. Imag.
Biol. 2012, 14 (1), 88-95.

5 . Perrin, D. M., F-18 -Organotrifluoroborates as Radioprosthetic Groups for PET Imaging: From Design Principles toPreclinical Applications. Acc. Chem. Res. 2016, 49 (7), 1333-1343.

6 . Pourghiasian, M.; Liu, Z. B.; Pan, J. H.; Zhang, Z. X.; Colpo, N.; Lin, K. S.; Perrin, D. M.; Benard, F., F-18-AmBF3-MJ9:
A novel radiofluorinated bombesin derivative for prostate cancer imaging. Biorg. Med. Chem. 2015, 23 (7), 1500-1506.

7 . Liu, Z. B.; Pourghiasian, M.; Benard, F.; Pan, J. H.; Lin, K. S.; Perrin, D. M., Preclinical Evaluation of a High-Affinity

F-18-Trifluoroborate Octreotate Derivative for Somatostatin Receptor Imaging. J. Nucl. Med. 2014, 55 (9), 1499-1505.

8 . Liu, Z. B.; Amouroux, G.; Zhang, Z. X.; Pan, J. H.; Hundal-Jabal, N.; Colpo, N.; Lau, J.; Perrin, D. M.; Benard, F.; Lin,K. S., F-18-Trifluoroborate Derivatives of Des-Arg(10) Kallidin for Imaging Bradykinin B1 Receptor Expression with
Positron Emission Tomography. Mol. Pharm. 2015, 12 (3), 974-982.

9 . Zhang, C.; Zhang, Z.; Lin, K.-S.; Lau, J.; Zeisler, J.; Colpo, N.; Perrin, D. M.; Benard, F., Melanoma Imaging Using
18F-Labeled alpha-Melanocyte-Stimulating Hormone Derivatives with Positron Emission Tomography. Mol. Pharm.
2018, 15 (6), 2116-2122.

10 . Liu, Z. B.; Radtke, M. A.; Wong, M. Q.; Lin, K. S.; Yapp, D. T.; Perrin, D. M., Dual Mode Fluorescent F-18-PET Tracers: Efficient
Modular Synthesis of Rhodamine-[cRGD](2)-[F-18]-Organotrifluoroborate, Rapid, and High Yielding One-Step F-18-Labeling at
High Specific Activity, and Correlated in Vivo PET Imaging and ex Vivo Fluorescence. Bioconjugate Chem. 2014, 25 (11), 1951-1962.

25

Ratmir Derda
University of Alberta

Contact : Ratmir@ualberta.ca

Research Interests
Molecular recognition and receptor-ligand interactions, genetically-encoded technologies in chemistry and biology,
discovery trajectories and reproducibility of molecular discovery, chemistry-information interface, emergence of complexity.

Education
2001
2008

B.Sc. in Physics, Moscow Institute of Physics and Technology
Ph.D. in Chemistry, University of Wisconsin-Madison

Professional Career1997 - 2001
2006 - 2011
2011 - present

Postdoctoral fellow, Harvard University, Wyss Institute of Biologically Inspired Engineering
Assistant Professor, Department of Chemistry, University of Alberta
Associate Professor, Department of Chemistry, University of Alberta

Scientific Activities
2017 - present

Founder and CEO 48Hour Discovery INC

Honors
1997
2011
2014
2016
2017
2018
2018

Gold Medal at the XXIX International Chemistry Olympiad, Montreal, Canada.
Canadian Rising Star in Global Health (from Grand Challenges Canada)
Boulder Peptide Society Young Investigator Award
Rising Star in Chemical Biology from International Chemical Biology Society
Martha Cook Piper Research Prize from University of Alberta
David Gin Award in Carbohydrate Chemistry from American Chemical Society
Melanie O’Neill Young Investigator Award in Biological Chemistry from CSC

Publications
S. Ng, et al. Genetically-encoded Fragment-based Discovery of Glycopeptide Ligands for Carbohydrate-binding Proteins, J. Am. Chem. Soc., 2015,

1. 137, 5248–5251

W. Matochko, S.C. Li, S.K.Y. Tang, R. Derda, Prospective identification of parasite sequences in phage display screens, Nuc. Acid. Res. 2014, 42,

2. 1784-98
26

Genetically-Encoded Technologies for
Discovery of Instructive Biomaterials
Ratmir Derda
University of Alberta

Interaction between extracellular ligands and cell-surface receptors is a fundamental mechanism for control of cellularresponses, homeostasis and differentiation. Discovery of new ligands that actuate cell surface receptors interaction is
the starting point for development of drugs and instructive biomaterials. Genetically-encoded (GE) molecular libraries,
such as Nobel prize-winning phage display technology, are poised to become the major source of discovery of
biological drugs and development of ligands. We employ organic chemistry to upgrade canonical GE-polypeptide
libraries restricted to 20 natural amino acids [1] and expand the use of GE-technologies to drug and material discovery.
Such discoveries necessitate development of new chemical scaffolds that do not break down in aggressive proteolytic
environment encountered in extracellular environment, serum or GI-tract. Using GE-libraries of peptides as a starting
material for multi-step organic synthesis [1], we produce GE-libraries of novel cyclic [2] or bicyclic [3] architectures thatexhibit remarkable stability to proteolytic degradation. We show that libraries of phage-displayed peptides can beapplied to discover ligands for receptors on the surface of cells. Ligand discovered in such campaigns can be
immobilized on 3D [4-5] or 2D substrates [6-8] to give rise to materials that control adhesion, growth, differentiationand self-renewal of stem cells.

References[ 1 ] S Ng, R. Derda “Genetically-Encoded Fragment-Based Discovery”, 2019, Curr. Op. Chem. Biol.
[ 2 ] R. Mukherjee, J. Y. K. Wong, V. Triana, M. Miskolzie, A. Henninot, J. J. Dwyer, R. Derda* “Aqueous Biocompatible
Bicyclization of Peptides with Two-fold Symmetric Linchpin”, in review[ 3 ] S. Kalhor-Monfared, M. R. Jafari, J. T. Patterson, P. I. Kitov, J. J. Dwyer, J. J. Nuss, R Derda “Rapid Biocompatible
Macrocyclization of Peptides with Decafluorosulfone” Chem. Sci., 2016, 7, 3785-3790[ 4 ] F. Deiss, W.L. Matochko, N. Govindasamy, E.Y. Lin, R Derda, “Flow-Through Synthesis on Teflon-Patterned Paper To
Produce Peptide Arrays for Cell-Based Assays”, Angew. Chemie Intl Ed. 2014, 53, 6374–6377[ 5 ] F. Deiss,PDF Y. Yang,UG W. L. Matochko,GS R. Derda* “Heat-enhanced peptide synthesis on Teflon-patterned paper“,
Org. Biolmol. Chem. 2016, 14, 5148-5156[ 6 ] E. Lin, A. Sikhand, J. Wickware, Y. Hao, R Derda* “Peptide Microarray Patterning for Controlling and Monitoring Cell
Growth” Acta Biomater., 2016, 34, 53–59[ 7 ] L. Li, J.R. Klim, R. Derda, A.H. Courtney, L.L. Kiessling*, “Spatial control of cell fate using synthetic surfaces topotentiate TGF-beta signaling” Proc. Natl. Acad. Sci. U.S.A., 2011, 108, 11745[ 8 ] R. Derda, S. Musah, B.P. Orner, J.R. Klim, L. Li, L.L. Kiessling* “High-throughput Discovery of Synthetic Surfacesthat Support Proliferation of Pluripotent Cells” J. Am. Chem. Soc. 2010, 132, 1289.

27

Amy Szuchmacher Blum
McGill University

Contact : amy.blum@mcgill.ca

Research Interests
Self-assembly, plasmonics, nanoparticles, iron oxide, metamaterials

Education
1994
2000

B.A. Chemistry (cum laude) Princeton University
Ph.D. Physical Chemistry University of Washington

Professional Career
2001 - 2003

National Research Council Postdoctoral Fellow, US Naval Research Laboratory

2003 - 2008

Research Chemist, US National Research Laboratory2008 - 2014

Assistant Professor, Department of Chemistry, McGill University

2014 - present

Associate Professor, Department of Chemistry, McGill University

Scientific Activities
2012 - present

Director, McGill QCAM AFM User Facility

2018 - 2020

ESF College of Expert Reviewers

Publications
Iron oxide surface chemistry: the effect of chemical structure on binding in benzoic acid and catechol derivatives, Katalin V. Korpany, Dorothy D.

1. Majewski, Cindy T. Chiu, Shoronia N. Cross, and Amy Szuchmacher Blum*. Langmuir, 33 (12), 3000-3013 (2017).

Nanoring formation via in-situ photoreduction of silver on a virus scaffold, Serene S. Bayram, Omar K. Zahr, Julia Del Re, and Amy Szuchmacher

2. Blum*. Nanotechnology, 27, 485603 (2016).

Quick and Spontaneous Self-Assembly of Silver Nanoparticles into Highly Anisotropic Superstructures. Serene S. Bayram, Klas Lindfors, and Amy

3. Szuchmacher Blum*. Beilstein Journal of Nanotechnology, 7, 1219-1228 (2016).

28

Plasmonics with Viruses
Amy Szuchmacher Blum
McGill University

Although there have been many advances in synthesizing nanoparticles, the assembly of these materials into
deterministic and controllable patterns remains a major challenge. Biological systems operate at the nanoscale,building structural components with great chemical specificity that enable the processes of life. These successes result
from billions of years of evolution. By adapting them to our needs, it is possible to utilize well-defined and well-controlled
scaffolds to produce materials with novel properties that result from precise ordering on the nanoscale, such as anegative index of refraction, signal enhancement for spectroscopy, or evanescent wave focusing for superlenses.
Utilizing viruses and viral proteins as templates is a relatively new idea that could have a large impact innanotechnology and bioengineering. This approach offers the promise of exquisite control for positioning on thenanoscale, since the position of each coat protein within a virus-like particle is precisely defined, and self-assembly into
homogenous micron-scale particles occurs spontaneously.
We use tobacco mosaic virus (TMV) coat protein as a template to self-assemble nanoparticles. This approach
uses spatial arrangement instead of nanoparticle size, shape, or composition to control optical properties through thecollective interactions between neighboring nanoparticles. Surface plasmons are resonant oscillations in the freeelectrons of a metal that are excited through interaction with light at the resonant wavelength. The effect of theseplasmons is to focus incident light at the resonant wavelength into very small volumes near metal surfaces, leading tovery intense local fields. In addition, these plasmonic oscillations can couple together, giving rise to more complex
modes like plasmonic ring resonances that can be used to tune their response to incident light.
Here, we present robust covalent techniques using TMV coat protein as a template to produce nanostructured
materials with novel properties. By exploiting the self-assembling properties and chemical addressability of TMV coatprotein, we can utilize site-directed mutagenesis and bioconjugation strategies to produce highly symmetricalplasmonic nanorings, as evidenced by transmission electron microscopy (TEM). Theoretical models suggest that theserings may display an induced magnetic response at optical frequencies, and ensemble spectroscopic measurements
reveal intriguing optical properties. Optical effects can be tuned by the introduction of a nanoparticle in the center ofthe rings through a pH dependent electrostatic interaction. Preliminary dark field scattering data, obtained forindividual surface bound ring structures, is remarkably consistent with ensemble measurements, demonstrating that theobserved optical properties arise from the ring structures. Thus, we show the utility of biotemplates in generating
nanostructured building blocks for advanced materials.

29

Kunio Matsumoto
Nano Life Science Institute (WPI-NanoLSI), Cancer Research Institute,
Kanazawa University
Contact : kmatsu@staff.kanazawa-u.ac.jp

Research Interests
HGF-MET pathway in regeneration and cancer progression, drug discovery by macrocyclic peptide,structural base of MET receptor activation

Education
1981
1983
1986

Faculty of Science, Kanazawa University
Graduate School of Science, Kanazawa University
Graduate School of Science, Osaka University (Ph.D.)

Professional Career1987 -1990
1990 -1993
1993 -1994
1994 - 2007
2007 - present2017 - present

Assistant Professor, Department of Dermatology, Osaka University
Assistant Professor, Department of Biology, Kyushu University
Assistant Professor, Biomedical Research Center, Osaka University
Associate Professor, Graduate School of Medicine, Osaka University
Professor, Cancer Research Institute, Kanazawa University
Professor, Nano Life Science Institute (WPI-NanoLSI), Kanazawa University

Honors
1992
1996
1997
2001
2006
2014

Academic Incitement Award of Japanese Industrial Hygiene Dermatology AssociationJB Award of the Japanese Biochemical Society
Incitement Award of the Japanese Cancer Association
The 3rd Bio Business Competition JAPAN, The Special Award
Nature Medicine-AnGes MG BioMedical Award (Main Award)
The Commendation for Science and Technology by MEXT, Prizes for Science and Technology

Publications
Sakai K, Passioura T, Sato H, Ito K, Umitsu M, Takagi J, Kato Y, Yano S, Furuhashi H, Shibata M, Suga H§, Matsumoto K§. Macrocycle peptide inhibits

1. hepatocyte growth factor by capturing its flexible multi-domains in a static conformation. Nat Chem Biol, 15: 598-606, 2019.

Miao W, Sakai K, Ozawa N, Nishiuchi T, Suzuki Y, Ito K, Morioka T, Umitsu M, Takagi J, Suga H, Matsumoto K. Cellular signaling and gene expression

2. profiles evoked by a bivalent macrocyclic peptide that serves as an artificial MET receptor agonist. Scientific Rep, 8: 16492, 2018.

Matsumoto K, Umitsu M, De Silva DM, Roy A, Bottaro DP. HGF-MET in cancer progression and biomarker discovery. Cancer Science,

3. 108: 296-307, 2017.

Adachi E, Sakai K, Nishiuchi T, Imamura R, Sato H, Matsumoto K. Cell-autonomous changes in Met receptor expression regulate the growth and4. metastatic characteristics in malignant melanoma. Oncotarget, 7: 70779-70793, 2016.

Ito K†, Sakai K†, Suzuki Y, Ozawa N, Hatta T, Natsume T, Matsumoto K§, Suga H§. Artificial human Met agonists based on macrocycle scaffolds.

5. Nat Commun, 6: 6373, 2015.
30

Macrocyclic Peptides Targeting HGF-MET
Kunio Matsumoto
Nano Life Science Institute (WPI-NanoLSI), and Cancer Research Institute, Kanazawa University

HGF (Hepatocyte Growth Factor), a bioactive protein composed of 697
amino acids, binds and activates its receptor MET (Fig. 1, 2). Activationof MET receptor drives mitogenesis (cell proliferation), motogenesis (cellmigration), morphogenesis (3-D tubulogenesis), and cell survival, thereby
participates in regeneration of damaged tissues. Clinical trials using
recombinant HGF protein are ongoing for treatment of spinal cord injury
and amyotrophic lateral sclerosis. On the other hand, aberrant activationof MET is associated with progression of cancer, particularly drug
resistance and invasion-metastasis. Therefore, promotion of HGF-MET
pathway become regeneration-based medicine, while the detection andinhibition of HGF-MET pathway become anti-cancer diagnosis andtherapeutics.
By RaPID (Random Peptide Integrated Discovery), an innovative drug
discovery platform, we obtained macrocyclic peptides that specificallybind to HGF or MET with 1-10 nM Kd values. The cross-linking of MET-binding
macrocyclic peptides conferred them an ability to selectively activate
MET [1-3]. These artificial MET-ligands exhibited mitogenic, motogenic,
and morphogenic activities that are comparable to native ligand HGF.
On the other hand, we obtained HGF-inhibitory peptide-8 (HiP-8) (Fig. 2)[4]. HiP-8 selectively recognizes and inhibits two-chain active HGF but
not single-chain precursor HGF. High-speed atomic force microscopy
analysis indicated that the binding of HiP-8 to HGF suppress dynamicd o m a i n m o v e m e n t o f H G F. U s i n g H i P - 8 a s a m o l e c u l a r p ro b e ,accumulation of tcHGF in cancer tissue could be detected by PET(Positron Emission Tomography) imaging. Selective detection and/or
inhibition of tcHGF by HiP-8 is expected to be better diagnosis and/or
therapeutics for drug discovery approach targeting HGF-MET.

References[ 1 ] Ito K†, Sakai K†, Suzuki Y, Ozawa N, Hatta T, Natsume T, Matsumoto K§, Suga H§. Artificial human Met agonists
based on macrocycle scaffolds. Nat Commun, 6: 6373, 2015.

[ 2 ] Miao W, Sakai K, Ozawa N, Nishiuchi T, Suzuki Y, Ito K, Morioka T, Umitsu M, Takagi J, Suga H, Matsumoto K.
Cellular signaling and gene expression profiles evoked by a bivalent macrocyclic peptide thatserves as an artificial MET receptor agonist. Scientific Rep, 8: 16492, 2018.
[ 3 ] Miao W, Sakai K, Imamura R, Ito K, Suga H, Sakuma T, Yamamoto T, Matsumoto K. MET activation bya macrocyclic peptide agonist couples to biological responses differently from HGF in a context-dependent
manner. Int J Mol Sci,19: 3141, 2018.
[ 4 ] Sakai K, Passioura T, Sato H, Ito K, Furuhashi H, Umitsu M, Takagi J, Kato Y, Mukai H, Warashina S, Zouda M,
Watanabe Y, Yano S, Shibata M, Suga H§, Matsumoto K§. Macrocyclic peptide-based inhibition and imaging of
hepatocyte growth factor. Nat Chem Biol, 15: 598-606, 2019.

31

Satoru Okuda
Nano Life Science Institute (WPI-NanoLSI), Kanazawa University
PRESTO, Japan Science and Technology Agency
Contact : satokuda@staff.kanazawa-u.ac.jp

Research Interests
Biomechanics, Multi-cellular dynamics, Multi-scale simulation, Morphogenesis, Collective cell motion

Education
2008
2010
2013

School of Engineering Science, Faculty of Engineering, Kyoto University
Department of Mechanical Engineering and Science, Grad. School of Engineering, Kyoto University
Department of Micro Engineering, Grad. School of Engineering, Kyoto University

Professional Career2010 - 2013

Pre-Doctoral Fellow DC1, Japan Society for the Promotion of Science2013 - 2016

Research Scientist, RIKEN Center for Developmental Biology

2016 - 2017

Special Postdoctoral Researcher, RIKEN Center for Developmental Biology

2016 - present

PRESTO Researcher, Japan Science and Technology Agency

2019 - present

Associate Professor, Nano Life Science Institute (WPI-NanoLSI), Kanazawa University

Honors2017
2017

Yamaguchi Medal, Asian-Pacific Association for Biomechanics
Encouragement Award, Japan Society of Mechanical Engineers

Publications
1. Okuda, et al, "Apical junctional fluctuations lead to cell flow while maintaining epithelial integrity," Biophysical Journal 116 (6): 1159-1170 (2019)
2. Okuda, et al, "Strain-triggered mechanical feedback in self-organizing optic cup morphogenesis," Science Advances 4(11): eaau1354 (2018)
Okuda, et al, "Combining Turing and 3D vertex models reproduces autonomous multicellular morphogenesis with undulation, tubulation,

3. and branching," Scientific Reports 8: 2386 (2018)32

Versatile modeling of three-dimensional multi-cellular dynamics:
in-silico and in-vitro combined approach toself-organizing morphogenesis
Satoru Okuda
Nano Life Science Institute (WPI-NanoLSI), Kanazawa University
PRESTO, Japan Science and Technology Agency

Organogenesis is a self-organizing process of multiple cells in three-dimensional (3D) space. This process is driven byintrinsic mechanisms of individual cells; nevertheless, macroscopic 3D tissue deformations are robustly regulated duringmorphogenesis. While such robust regulation of multicellular dynamics requires feedback from tissue deformations tocellular force generations, however, it is still unclear how individual cells sense 3D tissue deformations duringmorphogenesis. To address this issue, we developed a versatile 3D vertex model that enables the computational
simulation of 3D multicellular dynamics at the single-cell resolution. We then combined it with the unique culture
system of pluripotent stem cell-derived optic-cup organoids. This in vitro system recapitulates the step-wise process of
optic-cup formation. We measured several mechanical properties in vitro and introduced them into the model toperform quantitative simulations. Remarkably, computational simulations for unknown parameters predicted several key
cell behaviors. Based on the predictions, we carried out mechanical and pharmacological assays in vitro, which
revealed the crucial role of mechanical force in signaling between distant cells to trigger their next-step behaviors inthe sequential tissue deformations. We hereby conclude that 3D tissue deformation is fed back to cellular force
generation via mechanosensing, where mechanical force plays a key role in signaling between distant cells to robustly
regulate self-organizing morphogenesis [1].
In this talk, I will present the versatile 3D vertex model and its applications to the embryonic stem cell-derived
optic-cup formation and several other biological phenomena [1,2,3].

References[ 1 ] Okuda, et al, "Strain-triggered mechanical feedback in self-organizing optic cup morphogenesis,"
Science Advances 4(11): eaau1354 (2018)[ 2 ] Okuda, et al, "Apical junctional fluctuations lead to cell flow while maintaining epithelial integrity,"
Biophysical Journal 116 (6): 1159-1170 (2019)[ 3 ] Okuda, et al, "Combining Turing and 3D vertex models reproduces autonomous multicellular morphogenesis with
undulation, tubulation, and branching," Scientific Reports 8: 2386 (2018)33

Satoshi Toda
Department of Cellular and Molecular Pharmacology, Center for Systems
and Synthetic Biology, University of California San Francisco
Nano Life Science Institute (WPI-NanoLSI), Kanazawa University
Contact : stoda0317@gmail.com

Research Interests
I am interested in how the systems of molecular or cellular networks can achieve biological functions such as tissue
development. To address this question, I take a bottom-up approach: design, build and test molecular/cellular networks
to understand how they work and create useful products for applications.

Education
2009
2011
2014

B.Sc., Engineering (Kyoto University)
M.Sc., Life science (Kyoto University)
Ph. D., Medical science (Kyoto University)

Professional Career2014 - 2015

Postdoctoral fellow, Kyoto University

2015 - present

Postdoctoral fellow, University of California San Francisco

2019 - present
Oct. 2019 -Cooperative Researcher, Nano Life Science Institute (WPI-NanoLSI), Kanazawa University
Assistant Professor, Nano Life Science Institute (WPI-NanoLSI), Kanazawa University

Scientific Activities
2015 - 2016

Japan Society for the Promotion of Science (JSPS) Overseas Research Fellowship2016 - 2019

Human Frontier Science Program (HFSP) Long-Term Fellowship

Honors
2009
2012
2013

Hatakeyama Award (The Japan Society of Mechanical Engineers)
KMYIA Young Investigator Award (Kyoto University Faculty of Medicine)
Suzuki Koichi memorial award (The Japanese Biochemical Society)

Publications
Toda S, Brunger J, Lim WA. Synthetic development: learning to program multicellular self-organization.

1. Current Opinion in Systems Biology.14, 41–49 (2019)Toda S, Blauch LR, Tang SKY, Morsut L, Lim WA. Programming self-organizing multicellular structures with synthetic cell-cell signaling.

2. Science. 361, 156-162 (2018)34

Synthetic tissue formation:
Programming multicellular self-organization
Satoshi Toda
Department of Cellular and Molecular Pharmacology, Center for Systems and Synthetic Biology, University of California San Francisco
Nano Life Science Institute (WPI-NanoLSI), Kanazawa University

Multicellular animals emerge from a single fertilized cell that can differentiate into a multitude of diverse cell
types that spatially self-organize into 3D tissue architectures. All the necessary genetic circuits to develop complex
tissues and organs are written and stored as genomic DNA programs in the single cell. To understand how suchcompact genetic programs can encode algorithms that allow individual cells to build complex macroscale structures bythemselves, we need to rewrite and test genetic programs. A common theme in the self-organization of multicellulartissues is the use of cell-cell signaling networks to induce morphological changes. We have recently developed asynthetic Notch receptor (synNotch) system that allows us to engineer new orthogonal cell-cell signaling to control
transgene expression [1]. Using the modular synNotch platform, we engineered artificial genetic programs in which
specific cell-cell contacts induced changes in cadherin-based cell adhesion. Despite their simplicity, these minimal
intercellular programs were sufficient to yield multicellular assemblies with hallmarks of natural developmental systems:
robust self-organization, well-choreographed sequential assembly, cell type divergence, symmetry breaking, andregeneration upon injury [2]. These results demonstrate the flexibility and power of the modular synthetic system toprogram self-organizing structures. I will present a series of experiments to design and test synthetic self-organizing
structures and discuss next research directions towards constructive understanding of tissue formation.

References[ 1 ] Morsut L, Roybal KT, Xiong X, Gordley RM, Coyle SM, Thomson M, Lim WA., Cell., 2016, 164, 780-791.
[ 2 ] Toda S, Blauch LR, Tang SKY, Morsut L, Lim WA., Science., 2018, 361, 156–162.

35

Wendell Lim
University of California, San Francisco
Howard Hughes Medical InstituteContact : Tel 415-502-8080 E-Mail wendell.lim@ucsf.edu

Research Interests
My research focuses on the design principles of molecular circuits that govern cell decision-making and responses.

Education
1986
1991
1992 - 1996

Harvard University, Cambridge, MA

AB

Chemistry

MIT, Cambridge, MA			

PhD

Biochemistry and Biophysics

Yale University, New Haven, CT		

Postdoc Biophysics and Biochemistry

Professional Career1996 - 2000
2000 - 2003
2003 - present
2008 - present
2015 - present

Assistant Professor, Department of Cellular & Molecular Pharmacology, UCSF
Associate Professor, Department of Cellular & Molecular Pharmacology, UCSF
Professor, Department of Cellular & Molecular Pharmacology, UCSF
Investigator, Howard Hughes Medical Institute, San Francisco, CA
Chair, Department of Cellular & Molecular Pharmacology, UCSF

Honors1992 - 1994

Helen Hay Whitney Foundation Postdoctoral Fellowship

1997
1997
1997
2010
2012
2018

Burroughs Wellcome Fund New Investigator in the Pharmacological Sciences
Searle Foundation Scholar
David and Lucille Packard Fellow in Science and Engineering
Hans Neurath Award, Protein Society
Wired SmartList: 50 people who will change the world
Feodor Lynen Medal, German Society for Biochemistry and Molecular Biology

Publications
1. Morsut et al., Engineering Customized Cell Sensing and Response Behaviors Using Synthetic Notch Receptors. Cell, 2016.
2. Roybal et al., Precision Tumor Recognition by T Cells With Combinatorial Antigen Sensing Circuits. Cell, 2016.
3. Toda et al, Programming self-organizing multicellular structures with synthetic cell-cell signaling. Science, 2018.
36

Learning to program cellular machines
Wendell A. Lim, PhD
University of California, San Francisco
Howard Hughes Medical Institute

Living cells are remarkable machines capable of complex sensing, decision making and cooperation. We have been
pioneering synthetic biology approaches in which we ask how we can use simple molecular components to construct
and rewire cellular regulatory networks to engineer cells that perform novel functions, with the same precision androbustness of evolved systems. We have been applying these approaches to the challenge of engineering therapeutic
immune cells that can precisely recognize cancer (or other diseases) and execute robust and controlled therapeutic
programs.

37

Memo