Sasaki, Eita



Faculty of Pharmacy, Department of Pharmaceutical Sciences Analytical Chemistry for Drug Discovery (Shiba-Kyoritsu)


Project Senior Assistant Professor (Non-tenured)/Project Assistant Professor (Non-tenured)/Project Lecturer (Non-tenured)

E-mail Address

E-mail address

Related Websites

Contact Address

1-5-30 Shibakoen, Minato-ku, Tokyo 105-8512, Japan

Telephone No.


Career 【 Display / hide

  • 2011.06

    The University of Texas at Austin, College of Pharmacy, Postdoctoral Fellow

  • 2011.09

    The University of Tokyo, Graduate School of Pharmaceutical Sciences, Project Researcher

  • 2012.04

    ETH Zurich, Department of Chemistry and Applied Biosciences, JSPS Postdoctoral Fellow for Research Abroad

  • 2014.04

    ETH Zurich, Department of Chemistry and Applied Biosciences, Postdoctoral Fellow

  • 2017.04

    The University of Tokyo, Graduate School of Agricultural and Life Sciences, Assistant Professor

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Academic Background 【 Display / hide

  • 1999.04

    The University of Tokyo, Faculty of Pharmaceutical Sciences

    University, Graduated

  • 2003.04

    The University of Tokyo, Graduate School of Pharmaceutical Sciences

    Graduate School, Completed, Master's course

  • 2005.09

    The University of Texas at Austin, Department of Chemistry and Biochemistry

    U.S.A., Graduate School, Completed, Doctoral course

Licenses and Qualifications 【 Display / hide

  • Pharmacist, 2003.09


Research Areas 【 Display / hide

  • Chemical biology

  • Nanobioscience (Protein Engineering)

Research Keywords 【 Display / hide

  • protein cage

  • self-assembly

  • fluorescence probe

Research Themes 【 Display / hide

  • Design and Application of Protein Self-Assembly, 



Papers 【 Display / hide

  • Studies of lincosamide formation complete the biosynthetic pathway for lincomycin A

    SA Wang, CI Lin, J Zhang, R Ushimaru, E Sasaki, H Liu

    Proceedings of the National Academy of Sciences 117 (40), 24794-24801 (Proceedings of the National Academy of Sciences)   2020.09

    Research paper (scientific journal), Joint Work, Accepted,  ISSN  0027-8424

     View Summary

    The structure of lincomycin A consists of the unusual eight-carbon thiosugar core methyllincosamide (MTL) decorated with a pendent <italic>N</italic>-methylprolinyl moiety. Previous studies on MTL biosynthesis have suggested GDP-ᴅ-<italic>erythro</italic>-α-ᴅ-<italic>gluco</italic>-octose and GDP-ᴅ-α-ᴅ-lincosamide as key intermediates in the pathway. However, the enzyme-catalyzed reactions resulting in the conversion of GDP-ᴅ-<italic>erythro</italic>-α-ᴅ-<italic>gluco</italic>-octose to GDP-ᴅ-α-ᴅ-lincosamide have not yet been elucidated. Herein, a biosynthetic subpathway involving the activities of four enzymes—LmbM, LmbL, CcbZ, and CcbS (the LmbZ and LmbS equivalents in the closely related celesticetin pathway)—is reported. These enzymes catalyze the previously unknown biosynthetic steps including 6-epimerization, 6,8-dehydration, 4-epimerization, and 6-transamination that convert GDP-ᴅ-<italic>erythro</italic>-α-ᴅ-<italic>gluco</italic>-octose to GDP-ᴅ-α-ᴅ-lincosamide. Identification of these reactions completes the description of the entire lincomycin biosynthetic pathway. This work is significant since it not only resolves the missing link in octose core assembly of a thiosugar-containing natural product but also showcases the sophistication in catalytic logic of enzymes involved in carbohydrate transformations.

  • Self‐Assembly of Proteinaceous Shells around Positively Charged Gold Nanomaterials Enhances Colloidal Stability in High‐Ionic‐Strength Buffers

    E Sasaki, RM Dragoman, S Mantri, DN Dirin, MV Kovalenko, D Hilvert

    ChemBioChem 21 (1-2), 74-79 (Wiley)  21 ( 1-2 ) 74 - 79 2020.01

    Research paper (scientific journal), Joint Work, Accepted,  ISSN  1439-4227

  • Structure and Self-assembly of Negatively Supercharged Protein Cages

    Eita Sasaki, Donald Hilvert

    YAKUGAKU ZASSHI (Pharmaceutical Society of Japan)  139 ( 2 ) 199 - 208 2019.02

    Research paper (scientific journal), Single Work, Except for reviews,  ISSN  0031-6903

  • Expanding the structural analysis capabilities on an Orbitrap-based mass spectrometer for large macromolecular complexes

    KL Fort, M Van de Waterbeemd, D Boll, M Reinhardt-Szyba, ME Belov, ...

    Analyst 143 (1), 100-105 (Royal Society of Chemistry (RSC))  143 ( 1 ) 100 - 105 2018

    Research paper (scientific journal), Joint Work, Accepted,  ISSN  0003-2654

     View Summary

    <p>Native mass spectrometry can provide insight into the structure of macromolecular biological systems.</p>

  • Structure and assembly of scalable porous protein cages

    E Sasaki, D Böhringer, M van de Waterbeemd, M Leibundgut, ...

    Nature Communications 8, 14663 (NATURE PUBLISHING GROUP)  8   14663 2017.03

    Research paper (scientific journal), Joint Work, Accepted,  ISSN  2041-1723

     View Summary

    Proteins that self-assemble into regular shell-like polyhedra are useful, both in nature and in the laboratory, as molecular containers. Here we describe cryo-electron microscopy (EM) structures of two versatile encapsulation systems that exploit engineered electrostatic interactions for cargo loading. We show that increasing the number of negative charges on the lumenal surface of lumazine synthase, a protein that naturally assembles into a similar to 1-MDa dodecahedron composed of 12 pentamers, induces stepwise expansion of the native protein shell, giving rise to thermostable similar to 3-MDa and similar to 6-MDa assemblies containing 180 and 360 subunits, respectively. Remarkably, these expanded particles assume unprecedented tetrahedrally and icosahedrally symmetric structures constructed entirely from pentameric units. Large keyhole-shaped pores in the shell, not present in the wild-type capsid, enable diffusion-limited encapsulation of complementarily charged guests. The structures of these supercharged assemblies demonstrate how programmed electrostatic effects can be effectively harnessed to tailor the architecture and properties of protein cages.

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Reviews, Commentaries, etc. 【 Display / hide

  • Bottom-up construction of a synthetic carboxysome

    Shiksha Mantri, Raphael Frey, Marco Rocca, Eita Sasaki, Donald Hilvert

    PROTEIN SCIENCE (WILEY-BLACKWELL)  24   190 - 191 2015.10

    Summary of the papers read (international conference), Joint Work,  ISSN  0961-8368

  • Development of near-infrared fluorescent probes for in vivo imaging of nitric oxide

    E Sasaki, H Nishimatsu, Y Hirata, T Nagano


    Summary of the papers read (international conference), Joint Work,  ISSN  0065-7727

Research Projects of Competitive Funds, etc. 【 Display / hide

  • 多様な自然抗体と食を起源とする抗原の相互作用に関する研究


    The University of Tokyo, 佐々木 栄太, Grant-in-Aid for Early-Career Scientists

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  • メタボライト-シグナル連関による骨格筋恒常性維持機構の解明とその食品分野への応用


    The University of Tokyo, 山内 祥生, 佐々木 栄太, Grant-in-Aid for Scientific Research (B)

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  • Development of fluorescent probes for acrolein, a product of lipid peroxidation


    The University of Tokyo, Sasaki Eita, Grant-in-Aid for Research Activity Start-up

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    We designed and synthesized functional fluorescence probes whose spectroscopic properties are altered upon reaction with acrolein, a reactive aldehyde species produced in vivo. One of the designed probes possessing a 7-nitrobenzoxadiazole scaffold with aryl azide substituent reacted with acrolein. Since the reaction product showed substantially red-shifted absorbance spectrum, it is possible to excite only the product in the measurement of fluorescence to detect acrolein. However, these azide-based fluorescence probes were not very stable and converted to the corresponding amino compounds over time. Thus, we also investigated and designed another type of fluorescence probes by using Michael addition of a sulfhydryl group to acrolein.