Details of the Researcher

PHOTO

Hikaru Nakazawa
Section
Graduate School of Engineering
Job title
Associate Professor
Degree
  • 博士(工学)(長岡技術科学大学)

  • 修士(工学)(長岡技術科学大学)

Committee Memberships 4

  • 生物工学会北日本支部 北日本支部幹事

    2023/04 - Present

  • 日本農芸化学会 産学官学術交流委員

    2022/04 - Present

  • 日本農芸化学会 産学官若手交流会 さんわか

    2017/04 - 2022/03

  • 化学工学会 化工誌編集委員会 化工誌編集委員

    2017/04 - 2020/03

Professional Memberships 7

  • 日本抗体学会

    2022/10 - Present

  • 日本化学会

  • 農芸化学会

  • 生物物理学会

  • 化学工学会

  • 蛋白質科学会

  • 生物工学会

︎Show all ︎Show first 5

Research Interests 3

  • Bioengineering

  • Protein engineering

  • Enzyme engineering

Research Areas 1

  • Manufacturing technology (mechanical, electrical/electronic, chemical engineering) / Applied biofunctional and bioprocess engineering /

Awards 3

  1. Poster award by the 3rd international Workshop by the 174th Committee JSPS “Symbiosis of Biology and Nanodevices (2019)

    2019/08 the 174th Committee JSPS Smart interface design with ZnO binding VHH for plasmonic biosensor

  2. YABEC(Young Asian Biochemical Engineers’ Community) Poster Award

    2013/08 AFOB

  3. 第27回 セルラーゼ研究会, ポスター賞 第一等,

    2013/07 セルラーゼ研究会

Papers 62

  1. Design of Cyborg Proteins by Loop Region Replacement with Oligo(ethylene glycol): Exploring Suitable Mutations for Cyborg Protein Construction Using Machine Learning Peer-reviewed

    Wijak Yospanya, Akari Matsumura, Yukihiro Imasato, Tomoyuki Itou, Yusuke Aoki, Hikaru Nakazawa, Takashi Matsui, Takeshi Yokoyama, Mihoko Ui, Mitsuo Umetsu, Satoru Nagatoishi, Kouhei Tsumoto, Yoshikazu Tanaka, Kazushi Kinbara

    Bulletin of the Chemical Society of Japan 2024/09/02

    Publisher: Oxford University Press (OUP)

    DOI: 10.1093/bulcsj/uoae090  

    ISSN: 0009-2673

    eISSN: 1348-0634

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    Abstract We synthesized a “cyborg protein,” wherein a synthetic molecule partially substitutes the main peptide chain by linking two protein domains with a synthetic oligomer. Green fluorescent protein (GFP) served as the model for constructing the cyborg proteins. We prepared circularly permuted GFP (cpGFP) with new termini between β10 and β11, where the original N- and C-termini were linked by a cleavable peptide loop. The cyborg GFP was constructed from cpGFP by linking the β10 and β11 with oligo(ethylene glycol) using maleimide-cysteine couplings, followed by the enzymatic cleavage of the N- and C-termini linking loop by thrombin. With the help of machine learning, we were able to obtain the cpGFP mutants that significantly alter the fluorescence activity (53% increase) by thrombin treatment, which splits cpGFP into two fragments (fragmented-GFP), and by heat shock. When the cyborg GFP was constructed using this mutant, the fluorescence intensity increased by 13% after heat treatment, similar to cpGFP (33% increase), and the behavior was significantly different from that of the fragmented-GFP. This result suggests the possibility that the oligo(ethylene glycol) chain in the cyborg protein plays a similar role to the peptide in the main chain of the protein.

  2. Extensive antibody search with whole spectrum black-box optimization

    Andrejs Tučs, Tomoyuki Ito, Yoichi Kurumida, Sakiya Kawada, Hikaru Nakazawa, Yutaka Saito, Mitsuo Umetsu, Koji Tsuda

    Scientific Reports 14 (1) 2024/01/04

    Publisher: Springer Science and Business Media LLC

    DOI: 10.1038/s41598-023-51095-z  

    eISSN: 2045-2322

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    Abstract In designing functional biological sequences with machine learning, the activity predictor tends to be inaccurate due to shortage of data. Top ranked sequences are thus unlikely to contain effective ones. This paper proposes to take prediction stability into account to provide domain experts with a reasonable list of sequences to choose from. In our approach, multiple prediction models are trained by subsampling the training set and the multi-objective optimization problem, where one objective is the average activity and the other is the standard deviation, is solved. The Pareto front represents a list of sequences with the whole spectrum of activity and stability. Using this method, we designed VHH (Variable domain of Heavy chain of Heavy chain) antibodies based on the dataset obtained from deep mutational screening. To solve multi-objective optimization, we employed our sequence design software MOQA that uses quantum annealing. By applying several selection criteria to 19,778 designed sequences, five sequences were selected for wet-lab validation. One sequence, 16 mutations away from the closest training sequence, was successfully expressed and found to possess desired binding specificity. Our whole spectrum approach provides a balanced way of dealing with the prediction uncertainty, and can possibly be applied to extensive search of functional sequences.

  3. Recent research advances on non-linear phenomena in various biosystems

    Yutaka Tamaru, Shuji Nakanishi, Kenya Tanaka, Mitsuo Umetsu, Hikaru Nakazawa, Aruto Sugiyama, Tomoyuki Ito, Naofumi Shimokawa, Masahiro Takagi

    Journal of Bioscience and Bioengineering 136 (2) 75-86 2023/08

    Publisher: Elsevier BV

    DOI: 10.1016/j.jbiosc.2023.03.012  

    ISSN: 1389-1723

  4. Synthesis of epitope-targeting nanobody based on native protein-protein interactions for FtsZ filamentation suppressor. International-journal

    Hikaru Nakazawa, Taiji Katsuki, Takashi Matsui, Atsushi Tsugita, Takeshi Yokoyama, Tomoyuki Ito, Sakiya Kawada, Yoshikazu Tanaka, Mitsuo Umetsu

    Biotechnology journal e2300039 2023/07/17

    DOI: 10.1002/biot.202300039  

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    Phage display and biopanning are powerful tools for generating binding molecules for a specific target. However, the selection process based only on binding affinity provides no assurance for the antibody's affinity to the target epitope. In this study, we propose a molecular-evolution approach guided by native protein-protein interactions to generate epitope-targeting antibodies. The binding-site sequence in a native protein was grafted into a complementarity-determining region (CDR) in the nanobody, and a nonrelated CDR loop (in the grafted nanobody) was randomized to create a phage display library. In this construction of nanobodies by integrating graft and evolution technology (CAnIGET method), suitable grafting of the functional sequence added functionality to the nanobody, and the molecular-evolution approach enhanced the binding function to inhibit the native protein-protein interactions. To apply for biological tool with growth screening, model nanobodies with an affinity for filamenting temperature-sensitive mutant Z (FtsZ) from Staphylococcus aureus were constructed and completely inhibited the polymerization of FtsZ as a function. Consequently, the expression of these nanobodies drastically decreased the cell division rate. We demonstrate the potential of the CAnIGET method with the use of native protein-protein interactions for steady epitope-specific evolutionary engineering. This article is protected by copyright. All rights reserved.

  5. Selection of target-binding proteins from the information of weakly enriched phage display libraries by deep sequencing and machine learning. International-journal

    Tomoyuki Ito, Thuy Duong Nguyen, Yutaka Saito, Yoichi Kurumida, Hikaru Nakazawa, Sakiya Kawada, Hafumi Nishi, Koji Tsuda, Tomoshi Kameda, Mitsuo Umetsu

    mAbs 15 (1) 2168470-2168470 2023

    DOI: 10.1080/19420862.2023.2168470  

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    Despite the advances in surface-display systems for directed evolution, variants with high affinity are not always enriched due to undesirable biases that increase target-unrelated variants during biopanning. Here, our goal was to design a library containing improved variants from the information of the "weakly enriched" library where functional variants were weakly enriched. Deep sequencing for the previous biopanning result, where no functional antibody mimetics were experimentally identified, revealed that weak enrichment was partly due to undesirable biases during phage infection and amplification steps. The clustering analysis of the deep sequencing data from appropriate steps revealed no distinct sequence patterns, but a Bayesian machine learning model trained with the selected deep sequencing data supplied nine clusters with distinct sequence patterns. Phage libraries were designed on the basis of the sequence patterns identified, and four improved variants with target-specific affinity (EC50 = 80-277 nM) were identified by biopanning. The selection and use of deep sequencing data without undesirable bias enabled us to extract the information on prospective variants. In summary, the use of appropriate deep sequencing data and machine learning with the sequence data has the possibility of finding sequence space where functional variants are enriched.

  6. G6P-capturing molecules in the periplasm of Escherichia coli accelerate the shikimate pathway International-journal

    Ryosuke Fujiwara, Mariko Nakano, Yuuki Hirata, Chisako Otomo, Daisuke Nonaka, Sakiya Kawada, Hikaru Nakazawa, Mitsuo Umetsu, Tomokazu Shirai, Shuhei Noda, Tsutomu Tanaka, Akihiko Kondo

    Metabolic Engineering 72 68-81 2022/07

    Publisher: Elsevier BV

    DOI: 10.1016/j.ymben.2022.03.002  

    ISSN: 1096-7176

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    Escherichia coli, the most studied prokaryote, is an excellent host for producing valuable chemicals from renewable resources as it is easy to manipulate genetically. Since the periplasmic environment can be easily controlled externally, elucidating how the localization of specific proteins or small molecules in the periplasm affects metabolism may lead to bioproduction development using E. coli. We investigated metabolic changes and its mechanisms occurring when specific proteins are localized to the E. coli periplasm. We found that the periplasmic localization of β-glucosidase promoted the shikimate pathway involved in the synthesis of aromatic chemicals. The periplasmic localization of other proteins with an affinity for glucose-6-phosphate (G6P), such as inactivated mutants of Pgi, Zwf, and PhoA, similarly accelerated the shikimate pathway. Our results indicate that G6P is transported from the cytoplasm to the periplasm by the glucose transporter protein EIICBGlc, and then captured by β-glucosidase.

  7. A streamlined strain engineering workflow with genome-wide screening detects enhanced protein secretion in Komagataella phaffii Peer-reviewed

    Yoichiro Ito, Misa Ishigami, Goro Terai, Yasuyuki Nakamura, Noriko Hashiba, Teruyuki Nishi, Hikaru Nakazawa, Tomohisa Hasunuma, Kiyoshi Asai, Mitsuo Umetsu, Jun Ishii, Akihiko Kondo

    Communications Biology 5 (1) 561 2022/06

    Publisher: Springer Science and Business Media LLC

    DOI: 10.1038/s42003-022-03475-w  

    eISSN: 2399-3642

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    Abstract Expression of secreted recombinant proteins burdens the protein secretion machinery, limiting production. Here, we describe an approach to improving protein production by the non-conventional yeast Komagataella phaffii comprised of genome-wide screening for effective gene disruptions, combining them in a single strain, and recovering growth reduction by adaptive evolution. For the screen, we designed a multiwell-formatted, streamlined workflow to high-throughput assay of secretion of a single-chain small antibody, which is cumbersome to detect but serves as a good model of proteins that are difficult to secrete. Using the consolidated screening system, we evaluated >19,000 mutant strains from a mutant library prepared by a modified random gene-disruption method, and identified six factors for which disruption led to increased antibody production. We then combined the disruptions, up to quadruple gene knockouts, which appeared to contribute independently, in a single strain and observed an additive effect. Target protein and promoter were basically interchangeable for the effects of knockout genes screened. We finally used adaptive evolution to recover reduced cell growth by multiple gene knockouts and examine the possibility for further enhancing protein secretion. Our successful, three-part approach holds promise as a method for improving protein production by non-conventional microorganisms.

  8. Enzymatic ligation of an antibody and arginine 9 peptide for efficient and cell-specific siRNA delivery

    Yu Ando, Hikaru Nakazawa, Daisuke Miura, Maho Otake, Mitsuo Umetsu

    Scientific Reports 11 (1) 2021/12

    Publisher: Springer Science and Business Media LLC

    DOI: 10.1038/s41598-021-01331-1  

    eISSN: 2045-2322

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    Abstract A fusion protein comprising an antibody and a cationic peptide, such as arginine-9 (R9), is a candidate molecule for efficient and cell-specific delivery of siRNA into cells in order to reduce the side effects of nucleic acid drugs. However, their expression in bacterial hosts, required for their development, often fails, impeding research progress. In this study, we separately prepared anti-EGFR nanobodies with the K-tag sequence MRHKGS at the C-terminus and R9 with the Q-tag sequence LLQG at the N-terminus, and enzymatically ligated them in vitro by microbial transglutaminase to generate Nanobody-R9, which is not expressed as a fused protein in E. coli. Nanobody-R9 was synthesized at a maximum binding efficiency of 85.1%, without changing the binding affinity of the nanobody for the antigen. Nanobody-R9 successfully delivered siRNA into the cells, and the cellular influx of siRNA increased with increase in the ratio of Nanobody-R9 to siRNA. We further demonstrated that the Nanobody-R9–siRNA complex, at a 30:1 ratio, induced an approximately 58.6% reduction in the amount of target protein due to RNAi in mRNA compared to lipofectamine.

  9. Machine-Learning-Guided Library Design Cycle for Directed Evolution of Enzymes: The Effects of Training Data Composition on Sequence Space Exploration Peer-reviewed

    Yutaka Saito, Misaki Oikawa, Takumi Sato, Hikaru Nakazawa, Tomoyuki Ito, Tomoshi Kameda, Koji Tsuda, Mitsuo Umetsu

    ACS Catalysis 11 (23) 14615-14624 2021/12

    DOI: 10.1021/acscatal.1c03753  

    ISSN: 2155-5435

  10. Combination Informatic and Experimental Approach for Selecting Scaffold Proteins for Development as Antibody Mimetics

    Ito Tomoyuki, Nishi Hafumi, Kameda Tomoshi, Yoshida Mayu, Fukazawa Reito, Kawada Sakiya, Nakazawa Hikaru, Umetsu Mitsuo

    Chemistry Letters 50 (11) 1867-1871 2021

    Publisher: The Chemical Society of Japan

    DOI: 10.1246/cl.210443  

    ISSN: 0366-7022

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    <p>Antibody mimetics are proteins smaller than antibodies that have antigen-binding properties. Here, we used a combination of informatic selection and experimental verification to identify from a public database several candidate scaffold proteins. From those candidates, we selected a protein with high thermal stability, bacterial expression, and mutation tolerance and used molecular engineering and phage display selection techniques to develop the scaffold into an antibody mimetic with binding affinity for galactin-3, a biomarker of cancer and heart disease.</p>

  11. Association behavior and control of the quality of cancer therapeutic bispecific diabodies expressed in Escherichia coli Peer-reviewed

    Hikaru Nakazawa, Tomoko Onodera-Sugano, Aruto Sugiyama, Yoshikazu Tanaka, Takamitsu Hattori, Teppei Niide, Hiromi Ogata, Ryutaro Asano, Izumi Kumagai, Mitsuo Umetsu

    Biochemical Engineering Journal 160 107636-107636 2020/08/15

    Publisher: Elsevier BV

    DOI: 10.1016/j.bej.2020.107636  

    ISSN: 1369-703X

    eISSN: 1873-295X

  12. Chemically Crosslinked Bispecific Antibodies for Cancer Therapy: Breaking from the Structural Restrictions of the Genetic Fusion Approach. International-journal Peer-reviewed

    Asami Ueda, Mitsuo Umetsu, Takeshi Nakanishi, Kentaro Hashikami, Hikaru Nakazawa, Shuhei Hattori, Ryutaro Asano, Izumi Kumagai

    International journal of molecular sciences 21 (3) 2020/01/21

    DOI: 10.3390/ijms21030711  

    ISSN: 1661-6596

    eISSN: 1422-0067

  13. Identification of Indium Tin Oxide Nanoparticle-Binding Peptides via Phage Display and Biopanning Under Various Buffer Conditions. International-journal Peer-reviewed

    Hikaru Nakazawa, Mitsuo Umetsu, Tatsuya Hirose, Takamitsu Hattori, Izumi Kumagai

    Protein and peptide letters 27 (6) 557-566 2020

    DOI: 10.2174/0929866526666191113151934  

    ISSN: 0929-8665

    eISSN: 1875-5305

  14. Nanoparticle Assisted Remodeling of Proteotoxic SOD1 Mutants Alters the Biointerface of the Functional Interaction of Microtubules and Kinesin Motors Peer-reviewed

    Kyongwan Kim, Selvaraj Subramaniyam, Ahmad Galaleldeen, Hikaru Nakazawa, Mitsuo Umetsu, Winfried Teizer, Sanjib Bhattacharyya

    ACS Applied Bio Materials 2 (10) 4121-4128 2019/10/21

    DOI: 10.1021/acsabm.9b00501  

    eISSN: 2576-6422

  15. 抗体断片の熱安定性向上を目的としたバイオ情報を活用したライブラリーデザインサイクルの提案

    服部 修平, 本田 亜由美, 二井手 哲平, 中澤 光, 梅津 光央

    日本生物工学会大会講演要旨集 2019年 280-280 2019/08

    Publisher: (公社)日本生物工学会

  16. Complementary Design for Pairing between Two Types of Nanoparticles Mediated by a Bispecific Antibody: Bottom-Up Formation of Porous Materials from Nanoparticles. International-journal Peer-reviewed

    Teppei Niide, Noriyoshi Manabe, Hikaru Nakazawa, Kazuto Akagi, Takamitsu Hattori, Izumi Kumagai, Mitsuo Umetsu

    Langmuir : the ACS journal of surfaces and colloids 35 (8) 3067-3076 2019/02/26

    DOI: 10.1021/acs.langmuir.8b03687  

    ISSN: 0743-7463

    eISSN: 1520-5827

  17. Machine-Learning-Guided Mutagenesis for Directed Evolution of Fluorescent Proteins. International-journal Peer-reviewed

    Yutaka Saito, Misaki Oikawa, Hikaru Nakazawa, Teppei Niide, Tomoshi Kameda, Koji Tsuda, Mitsuo Umetsu

    ACS synthetic biology 7 (9) 2014-2022 2018/09/21

    DOI: 10.1021/acssynbio.8b00155  

    ISSN: 2161-5063

    eISSN: 2161-5063

  18. 抗体データベースを利用した熱安定性向上と発現量向上に向けた大規模変異導入プロセスの開発

    服部 修平, 本田 亜由美, 二井手 哲平, 中澤 光, 梅津 光央

    日本生物工学会大会講演要旨集 平成30年度 157-157 2018/08

    Publisher: (公社)日本生物工学会

  19. High-throughput cytotoxicity and antigen-binding assay for screening small bispecific antibodies without purification. Peer-reviewed

    Aruto Sugiyama, Mitsuo Umetsu, Hikaru Nakazawa, Teppei Niide, Ryutaro Asano, Takamitsu Hattori, Izumi Kumagai

    Journal of bioscience and bioengineering 126 (2) 153-161 2018/08

    DOI: 10.1016/j.jbiosc.2018.02.007  

    ISSN: 1389-1723

    eISSN: 1347-4421

  20. Impact in stability during sequential CDR grafting to construct camelid VHH antibodies against zinc oxide and gold. International-journal Peer-reviewed

    Ryota Saito, Yutaro Saito, Hikaru Nakazawa, Takamitsu Hattori, Izumi Kumagai, Mitsuo Umetsu, Koki Makabe

    Journal of biochemistry 164 (1) 21-25 2018/07/01

    DOI: 10.1093/jb/mvy016  

    ISSN: 0021-924X

    eISSN: 1756-2651

  21. Compact Seahorse-Shaped T Cell-Activating Antibody for Cancer Therapy Peer-reviewed

    Fujii, H, Tanaka, Y, Nakazawa, H, Sugiyama, A, Manabe, N, Shinoda, A, Shimizu, N, Hattori, T, Hosokawa, K, Sujino, T, Ito, T, Niide, T, Asano, R, Kumagai, I, Umetsu, M

    Adv. Therapeut. 1 (1700031) 1700031-1700031 2018/06

    Publisher: Wiley

    DOI: 10.1002/adtp.201700031  

    ISSN: 2366-3987

    eISSN: 2366-3987

  22. Large-scale chirality in an active layer of microtubules and kinesin motor proteins. International-journal Peer-reviewed

    Kyongwan Kim, Natsuhiko Yoshinaga, Sanjib Bhattacharyya, Hikaru Nakazawa, Mitsuo Umetsu, Winfried Teizer

    Soft matter 14 (17) 3221-3231 2018/05/02

    Publisher: Royal Society of Chemistry

    DOI: 10.1039/c7sm02298k  

    ISSN: 1744-683X

    eISSN: 1744-6848

  23. Use of a Phage-Display Method to Identify Peptides that Bind to a Tin Oxide Nanosheets. International-journal Peer-reviewed

    Hikaru Nakazawa, Yasuko Seta, Tatsuya Hirose, Yoshitake Masuda, Mitsuo Umetsu

    Protein and peptide letters 25 (1) 68-75 2018

    Publisher: Bentham Science Publishers B.V.

    DOI: 10.2174/0929866525666171206114429  

    ISSN: 0929-8665

    eISSN: 1875-5305

  24. A semi high-throughput method for screening small bispecific antibodies with high cytotoxicity. International-journal Peer-reviewed

    Aruto Sugiyama, Mitsuo Umetsu, Hikaru Nakazawa, Teppei Niide, Tomoko Onodera, Katsuhiro Hosokawa, Shuhei Hattori, Ryutaro Asano, Izumi Kumagai

    Scientific reports 7 (1) 2862-2862 2017/06/06

    DOI: 10.1038/s41598-017-03101-4  

    ISSN: 2045-2322

    eISSN: 2045-2322

  25. Combination of molecular evolution and conformational information for antibody mimic

    Umetsu Mitsuo, Nakazawa Hikaru, Niide Teppei

    MEDCHEM NEWS 27 (1) 25-29 2017/02/01

    Publisher: The Pharmaceutical Society of Japan

    DOI: 10.14894/medchem.27.1_25  

    ISSN: 2432-8618

    eISSN: 2432-8626

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    Advance in library approach and accumulation of conformational information of proteins are causing drastic changes of protein engineering. Flexible design for the combination of amino acids appearing in library and easy access to conformational information enable us to draw up effective and dense libraries to express a new function on non-functional protein. Here, we show the creation of a protein with a new function, especially molecular recognition, by means of library approach and conformational information of proteins.

  26. 親和性ペプチド分子による有機結晶の構造制御と生体分子-半導体有機結晶ハイブリッド材料作製プロセスの開発

    二井手 哲平, 中澤 光, 梅津 光央

    ケミカルエンジニヤリング 62 23-27 2017

  27. Generation of camelid VHH bispecific constructs via in-cell intein-mediated protein trans-splicing. International-journal Peer-reviewed

    Yuki Shibuya, Natsuki Haga, Ryutaro Asano, Hikaru Nakazawa, Takamitsu Hattori, Daisuke Takeda, Aruto Sugiyama, Reiko Kurotani, Izumi Kumagai, Mitsuo Umetsu, Koki Makabe

    Protein engineering, design & selection : PEDS 30 (1) 15-21 2017/01

    DOI: 10.1093/protein/gzw057  

    ISSN: 1741-0126

    eISSN: 1741-0134

  28. Modulating the microtubule-tau interactions in biomotility systems by altering the chemical environment Peer-reviewed

    S. Bhattacharyya, K. Kim, H. Nakazawa, M. Umetsu, W. Teizer

    Integrative Biology (United Kingdom) 8 (12) 1296-1300 2016/12

    DOI: 10.1039/c6ib00182c  

    ISSN: 1757-9694

    eISSN: 1757-9708

  29. Altering the microtubule kinesin nanomechanics in the presence of metallic ions Peer-reviewed

    Sanjib Bhattacharyya, Kyongwan Kim, Hikaru Nakazawa, Mitsuo Umetsu, Winfried Teizer

    16th International Conference on Nanotechnology - IEEE NANO 2016 79-81 2016/11/21

    DOI: 10.1109/NANO.2016.7751410  

  30. Salt-Switchable Artificial Cellulase Regulated by a DNA Aptamer. International-journal Peer-reviewed

    Mari Takahara, Geisa Aparecida Lopes Gonçalves Budinova, Hikaru Nakazawa, Yutaro Mori, Mitsuo Umetsu, Noriho Kamiya

    Biomacromolecules 17 (10) 3356-3362 2016/10/10

    DOI: 10.1021/acs.biomac.6b01141  

    ISSN: 1525-7797

    eISSN: 1526-4602

  31. Contributions of loop histidine residues for Zinc ion binding and its stability of an anti-ZnO VHH antibody Peer-reviewed

    Ryosuke Sasaki, Hikaru Nakazawa, Izumi Kumagai, Mitsuo Umetsu, Koki Makabe

    PROTEIN SCIENCE 25 (S1) 168-168 2016/10

    ISSN: 0961-8368

    eISSN: 1469-896X

  32. Isomorphic coalescence of aster cores formed in vitro from microtubules and kinesin motors Peer-reviewed

    K. Kim, A. Sikora, H. Nakazawa, M. Umetsu, W. Hwang, W. Teizer

    Physical Biology 13 (5) 2016/09/21

    DOI: 10.1088/1478-3975/13/5/056002  

    ISSN: 1478-3967

    eISSN: 1478-3975

  33. Interleukin-6 Detection with a Plasmonic Chip Peer-reviewed

    Keiko Tawa, Masashi Sumiya, Mana Toma, Chisato Sasakawa, Takuma Sujino, Tatsuki Miyaki, Hikaru Nakazawa, Mitsuo Umetsu

    JOURNAL OF MOLECULAR AND ENGINEERING MATERIALS 4 (3) 1640009 2016/09

    DOI: 10.1142/S2251237316400098  

    ISSN: 2251-2373

    eISSN: 2251-2381

  34. One-dimensional assembly of functional proteins: Toward the design of an artificial cellulosome Peer-reviewed

    Y. Mori, H. Nakazawa, G. A.L. Gonçalves, T. Tanaka, M. Umetsu, N. Kamiya

    Molecular Systems Design and Engineering 1 (1) 66-73 2016

    DOI: 10.1039/c5me00011d  

    eISSN: 2058-9689

  35. A high performance Trichoderma reesei strain that reveals the importance of xylanase III in cellulosic biomass conversion. International-journal Peer-reviewed

    Hikaru Nakazawa, Tetsushi Kawai, Noriko Ida, Yosuke Shida, Kouki Shioya, Yoshinori Kobayashi, Hirofumi Okada, Shuji Tani, Jun-Ichi Sumitani, Takashi Kawaguchi, Yasushi Morikawa, Wataru Ogasawara

    Enzyme and microbial technology 82 89-95 2016/01

    DOI: 10.1016/j.enzmictec.2015.08.019  

    ISSN: 0141-0229

    eISSN: 1879-0909

  36. Heterologously expressed Aspergillus aculeatus β-glucosidase in Saccharomyces cerevisiae is a cost-effective alternative to commercial supplementation of β-glucosidase in industrial ethanol production using Trichoderma reesei cellulases. Peer-reviewed

    Treesukon Treebupachatsakul, Hikaru Nakazawa, Hideaki Shinbo, Hiroki Fujikawa, Asami Nagaiwa, Nobuhiro Ochiai, Takashi Kawaguchi, Mitsuru Nikaido, Kazuhide Totani, Koki Shioya, Yosuke Shida, Yasushi Morikawa, Wataru Ogasawara, Hirofumi Okada

    Journal of bioscience and bioengineering 121 (1) 27-35 2016/01

    DOI: 10.1016/j.jbiosc.2015.05.002  

    ISSN: 1389-1723

    eISSN: 1347-4421

  37. Characterization of two endoglucanases for the classification of the earthworm, Eisenia fetida Waki. International-journal Peer-reviewed

    Shin-ichi Akazawa, Yuki Ikarashi, Jun Yarimizu, Keisuke Yokoyama, Tomoya Kobayashi, Hikaru Nakazawa, Wataru Ogasawara, Yasushi Morikawa

    Bioscience, biotechnology, and biochemistry 80 (1) 55-66 2016

    DOI: 10.1080/09168451.2015.1075860  

    ISSN: 0916-8451

    eISSN: 1347-6947

  38. Organic crystal-binding peptides: morphology control and one-pot formation of protein-displaying organic crystals. International-journal Peer-reviewed

    Teppei Niide, Kyohei Ozawa, Hikaru Nakazawa, Daniel Oliveira, Hitoshi Kasai, Mari Onodera, Ryutaro Asano, Izumi Kumagai, Mitsuo Umetsu

    Nanoscale 7 (47) 20155-63 2015/12/21

    DOI: 10.1039/c5nr06471f  

    ISSN: 2040-3364

    eISSN: 2040-3372

  39. Utilization of recombinant Trichoderma reesei expressing Aspergillus aculeatus β-glucosidase I (JN11) for a more economical production of ethanol from lignocellulosic biomass. Peer-reviewed

    Treesukon Treebupachatsakul, Koki Shioya, Hikaru Nakazawa, Takashi Kawaguchi, Yasushi Morikawa, Yosuke Shida, Wataru Ogasawara, Hirofumi Okada

    Journal of bioscience and bioengineering 120 (6) 657-65 2015/12

    DOI: 10.1016/j.jbiosc.2015.04.015  

    ISSN: 1389-1723

    eISSN: 1347-4421

  40. Behavior of Kinesin Driven Quantum Dots Trapped in a Microtubule Loop. International-journal Peer-reviewed

    Aurélien Sikora, Filippo Federici Canova, Kyongwan Kim, Hikaru Nakazawa, Mitsuo Umetsu, Izumi Kumagai, Tadafumi Adschiri, Wonmuk Hwang, Winfried Teizer

    ACS nano 9 (11) 11003-13 2015/11/24

    DOI: 10.1021/acsnano.5b04348  

    ISSN: 1936-0851

    eISSN: 1936-086X

  41. Zinc Ion-binding Activity of an Anti-ZnO VHH Antibody, 4F2 Peer-reviewed

    Ryosuke Sasaki, Soichiro Kitazawa, Ryo Kitahara, Hikaru Nakazawa, Yoshikazu Tanaka, Izumi Kumagai, Mitsuo Umetsu, Koki Makabe

    CHEMISTRY LETTERS 44 (10) 1309-1311 2015/10

    DOI: 10.1246/cl.150537  

    ISSN: 0366-7022

    eISSN: 1348-0715

  42. Microtubule guiding in a multi-walled carbon nanotube circuit Peer-reviewed

    Aurélien Sikora, Javier Ramón-Azcón, Mustafa Sen, Kyongwan Kim, Hikaru Nakazawa, Mitsuo Umetsu, Izumi Kumagai, Hitoshi Shiku, Tomokazu Matsue, Winfried Teizer

    Biomedical Microdevices 17 (4) 2015/08

    Publisher: Springer Science and Business Media LLC

    DOI: 10.1007/s10544-015-9978-1  

    ISSN: 1387-2176

    eISSN: 1572-8781

  43. Microtubule guiding in a multi-walled carbon nanotube circuit. International-journal Peer-reviewed

    Aurélien Sikora, Javier Ramón-Azcón, Mustafa Sen, Kyongwan Kim, Hikaru Nakazawa, Mitsuo Umetsu, Izumi Kumagai, Hitoshi Shiku, Tomokazu Matsue, Winfried Teizer

    Biomedical microdevices 17 (4) 78-78 2015/08

    DOI: 10.1007/s10544-015-9978-1  

    ISSN: 1387-2176

    eISSN: 1572-8781

  44. ナノの発想からの新しい酵素複合体設計:ハイブリッドナノセルロソーム

    梅津 光央, 中澤 光

    酵素工学ニュース 72 10-14 2014/10

    Publisher: 酵素工学研究会

  45. Functional localization of kinesin/microtubule-based motility system along metallic glass microwires Peer-reviewed

    K. Kim, A. Sikora, K. S. Nakayama, H. Nakazawa, M. Umetsu, W. Hwang, W. Teizer

    APPLIED PHYSICS LETTERS 105 (14) 1-5 2014/10

    DOI: 10.1063/1.4896964  

    ISSN: 0003-6951

    eISSN: 1077-3118

  46. Microtubule shuttles on kinesin-coated glass micro-wire tracks. International-journal Peer-reviewed

    Kyongwan Kim, Andrew L Liao, Aurélien Sikora, Daniel Oliveira, Hikaru Nakazawa, Mitsuo Umetsu, Izumi Kumagai, Tadafumi Adschiri, Wonmuk Hwang, Winfried Teizer

    Biomedical microdevices 16 (4) 501-8 2014/08

    DOI: 10.1007/s10544-014-9852-6  

    ISSN: 1387-2176

    eISSN: 1572-8781

  47. Molecular motor-powered shuttles along multi-walled carbon nanotube tracks. International-journal Peer-reviewed

    Aurélien Sikora, Javier Ramón-Azcón, Kyongwan Kim, Kelley Reaves, Hikaru Nakazawa, Mitsuo Umetsu, Izumi Kumagai, Tadafumi Adschiri, Hitoshi Shiku, Tomokazu Matsue, Wonmuk Hwang, Winfried Teizer

    Nano letters 14 (2) 876-81 2014/02/12

    DOI: 10.1021/nl4042388  

    ISSN: 1530-6984

    eISSN: 1530-6992

  48. Detection of Brain-Derived Neurotrophic Factor (BDNF) with a Sandwich Assay on a Plasmonic Chip

    Mari Satoh, Keiko Tawa, Koichi Uegaki, Tomoko Hara, Mitsuo Umetsu, Hikaru Nakazawa, Makoto Itakura, Masami Takahashi, Hiroyuki Aota, Masami Kojima

    Transactions of the Materials Research Society of Japan 39 (3) 361-364 2014

    Publisher: The Materials Research Society of Japan

    DOI: 10.14723/tmrsj.39.361  

    ISSN: 1382-3469

    eISSN: 2188-1650

  49. 2P086 Smart interface antibody design for biosensor(01F. Protein: Engineering,Poster,The 52nd Annual Meeting of the Biophysical Society of Japan(BSJ2014))

    Sujino Takuma, Nakazawa Hikaru, Tawa Keiko, Asano Ryutaro, Kumagai Izumi, Umetsu Mitsuo

    Seibutsu Butsuri 54 (1) S209 2014

    Publisher: The Biophysical Society of Japan General Incorporated Association

    DOI: 10.2142/biophys.54.S209_2  

  50. Application of 300x Enhanced Fluorescence on a Plasmonic Chip Modified with a Bispecific Antibody to a Sensitive lmmunosensor Peer-reviewed

    Keiko Tawa, Mitsuo Umetsu, Hikaru Nakazawa, Takamitsu Hattori, Izumi Kumagai

    ACS APPLIED MATERIALS & INTERFACES 5 (17) 8628-8632 2013/09

    DOI: 10.1021/am402173y  

    ISSN: 1944-8244

  51. A comprehensive analysis of the effects of the main component enzymes of cellulase derived from Trichoderma reesei on biomass saccharification Peer-reviewed

    Tetsushi Kawai, Hikaru Nakazawa, Noriko Ida, Hirofumi Okada, Wataru Ogasawara, Yasushi Morikawa, Yoshinori Kobayashi

    Journal of Industrial Microbiology and Biotechnology 40 (8) 805-810 2013/08

    DOI: 10.1007/s10295-013-1290-6  

    ISSN: 1367-5435 1476-5535

  52. Rapid and Sensitive Detection of Brain-Derived Neurotrophic Factor with a Plasmonic Chip Peer-reviewed

    Keiko Tawa, Mari Satoh, Koichi Uegaki, Tomoko Hara, Masami Kojima, Haruko Kumanogoh, Hiroyuki Aota, Yoshiki Yokota, Takahiko Nakaoki, Mitsuo Umetsu, Hikaru Nakazawa, Izumi Kumagai

    JAPANESE JOURNAL OF APPLIED PHYSICS 52 (6) UNSP 06GK01 2013/06

    DOI: 10.7567/JJAP.52.06GK01  

    ISSN: 0021-4922

    eISSN: 1347-4065

  53. 2P089 Evolutional cellulosome design from module library(01F. Protein: Engineering,Poster)

    Nakazawa Hikaru, Ishigaki Yuri, Kobayashi Eiko, Kim Do-Myoung, Umetsu Mitsuo

    Seibutsu Butsuri 53 (1) S173 2013

    Publisher: The Biophysical Society of Japan General Incorporated Association

    DOI: 10.2142/biophys.53.S173_5  

  54. Biomass-binding peptides designed by molecular evolution for efficient degradation of cellulose in biomass by cellulase Peer-reviewed

    Hikaru Nakazawa, Akinori Ikeuchi, Do-Myoung Kim, Yuri Ishigaki, Hidetaka Asano, Katsunori Kouda, Izumi Kumagai, Mitsuo Umetsu

    GREEN CHEMISTRY 15 (2) 365-369 2013

    DOI: 10.1039/c2gc36914a  

    ISSN: 1463-9262

  55. In-one-pot-at-a-time ligation for high-throughput construction of a protein expression vector library Peer-reviewed

    Hikaru Nakazawa, Rui Todokoro, Yuri Ishigaki, Izumi Kumagai, Mitsuo Umetsu

    Chemistry Letters 42 (4) 424-426 2013

    DOI: 10.1246/cl.130014  

    ISSN: 0366-7022 1348-0715

  56. Hybrid nanocellulosome design from cellulase modules on nanoparticles: Synergistic effect of catalytically divergent cellulase modules on cellulose degradation activity Peer-reviewed

    Hikaru Nakazawa, Do-Myoung Kim, Takashi Matsuyama, Nobuhiro Ishida, Akinori Ikeuchi, Yuri Ishigaki, Izumi Kumagai, Mitsuo Umetsu

    ACS Catalysis 3 (6) 1342-1348 2013

    DOI: 10.1021/cs400012v  

    ISSN: 2155-5435

  57. Analysis of the saccharification capability of high-functional cellulase JN11 for various pretreated biomasses through a comparison with commercially available counterparts Peer-reviewed

    Tetsushi Kawai, Hikaru Nakazawa, Noriko Ida, Hirofumi Okada, Shuji Tani, Jun-ichi Sumitani, Takashi Kawaguchi, Wataru Ogasawara, Yasushi Morikawa, Yoshinori Kobayashi

    JOURNAL OF INDUSTRIAL MICROBIOLOGY & BIOTECHNOLOGY 39 (12) 1741-1749 2012/12

    DOI: 10.1007/s10295-012-1195-9  

    ISSN: 1367-5435

  58. 1C1510 Hybrid nano-cellulosome: functional analysis of various cellulose binding module as component of artificial cellulosome(Proteins: Measurement, Analysis, Engineering,Oral Presentation,The 50th Annual Meeting of the Biophysical Society of Japan)

    Nakazawa Hikaru, Kim Do-myoung, Matuyama Takashi, Ishida Nobuhiro, Ikeuchi Akinori, Kumagai Izumi, Umetsu Mitsuo

    Seibutsu Butsuri 52 S23-S24 2012

    Publisher: The Biophysical Society of Japan General Incorporated Association

    DOI: 10.2142/biophys.52.S23_5  

  59. A nanocluster design for the construction of artificial cellulosomes Peer-reviewed

    Do-Myoung Kim, Hikaru Nakazawa, Mitsuo Umetsu, Takashi Matsuyama, Nobuhiro Ishida, Akinori Ikeuchi, Haruo Takahashi, Ryutaro Asano, Izumi Kumagai

    CATALYSIS SCIENCE & TECHNOLOGY 2 (3) 499-503 2012

    DOI: 10.1039/c2cy00371f  

    ISSN: 2044-4753

  60. Construction of a recombinant Trichoderma reesei strain expressing Aspergillus aculeatus ss-glucosidase 1 for efficient biomass conversion Peer-reviewed

    Hikaru Nakazawa, Tetsushi Kawai, Noriko Ida, Yosuke Shida, Yoshinori Kobayashi, Hirofumi Okada, Shuji Tani, Jun-ichi Sumitani, Takashi Kawaguchi, Yasushi Morikawa, Wataru Ogasawara

    BIOTECHNOLOGY AND BIOENGINEERING 109 (1) 92-99 2012/01

    DOI: 10.1002/bit.23296  

    ISSN: 0006-3592

    eISSN: 1097-0290

  61. Directed evolution of endoglucanase III (Cel12A) from Trichoderma reesei Peer-reviewed

    Hikaru Nakazawa, Katsunori Okada, Tomoko Onodera, Wataru Ogasawara, Hirofumi Okada, Yasushi Morikawa

    APPLIED MICROBIOLOGY AND BIOTECHNOLOGY 83 (4) 649-657 2009/06

    DOI: 10.1007/s00253-009-1901-3  

    ISSN: 0175-7598

    eISSN: 1432-0614

  62. Characterization of the catalytic domains of Trichoderma reesei endoglucanase I, II, and III, expressed in Escherichia coli Peer-reviewed

    Hikaru Nakazawa, Katsunori Okada, Ryota Kobayashi, Tetsuya Kubota, Tomoko Onodera, Nobuhiro Ochiai, Naoki Omata, Wataru Ogasawara, Hirofumi Okada, Yasushi Morikawa

    APPLIED MICROBIOLOGY AND BIOTECHNOLOGY 81 (4) 681-689 2008/12

    DOI: 10.1007/s00253-008-1667-z  

    ISSN: 0175-7598

    eISSN: 1432-0614

Show all ︎Show first 5

Misc. 59

  1. 光-熱変換ナノ粒子を用いた太陽光応答型酵素活性化デバイス

    中澤光, 二井手哲平, 石垣友理, 梅津光央

    日本蛋白質科学会年会(Web) 24th 2024

  2. FtsZのネイティブタンパク質間相互作用から発想するエピトープターゲティング抗体設計

    中澤光, 勝木泰司, 松井崇, 田中良和, 梅津光央

    日本抗体学会学術大会プログラム・抄録集(Web) 2nd 2023

  3. Synthesis of epitope-targeting antibody based on native Protein-Protein interaction

    中澤光, 勝木泰司, 松井崇, 田中良和, 梅津光央

    日本生物工学会大会講演要旨集 75th 2023

  4. 細胞選択的RNAiを誘発する抗体-膜貫通ペプチド酵素的架橋設計

    中澤光, 勝木泰司, 松井崇, 田中良和, 梅津光央

    日本抗体学会学術大会プログラム・抄録集(Web) 1st 2022

  5. FtsZのネイティブタンパク質間相互作用から発想するエピトープターゲティング抗体設計

    中澤光, 勝木泰司, 松井崇, 田中良和, 梅津光央

    化学工学会秋季大会研究発表講演要旨集(CD-ROM) 53rd 2022

  6. Hybrid Nanoassembly via Material-binding Peptides and Proteins

    梅津光央, 中澤光, 二井手哲平

    Bio Industry 39 (3) 2022

    ISSN: 0910-6545

  7. Application of Next-Generation Sequencing Analysis in the Directed Evolution for Creating Antibody Mimic

    Tomoyuki Ito, Hafumi Nishi, Thuy Duong Nguyen, Yutaka Saito, Tomoshi Kameda, Hikaru Nakazawa, Koji Tsuda, Mitsuo Umetsu

    BIOPHYSICAL JOURNAL 120 (3) 87A-87A 2021/02

    ISSN: 0006-3495

    eISSN: 1542-0086

  8. そのエピトープは創薬標的となりえるか?:天然タンパク質の相互作用情報を利用したツール抗体設計

    勝木泰司, 中澤光, 松井崇, 田中良和, 梅津光央

    化学工学会秋季大会研究発表講演要旨集(CD-ROM) 51st 2020

  9. MACHINE-LEARNING-GUIDED MUTAGENESIS FOR DIRECTED EVOLUTION OF FLUORESCENT PROTEINS

    Tomoshi Kameda, Yutaka Saito, Misaki Oikawa, Hikaru Nakazawa, Teppei Niide, Koji Tsuda, Mitsuo Umetsu

    PROTEIN SCIENCE 28 203-204 2019/09

    ISSN: 0961-8368

    eISSN: 1469-896X

  10. 機械学習支援によるタンパク質進化工学検証:GFPからYFPへ

    及川未早来, 齋藤裕, 亀田倫史, 中澤光, 二井手哲平, 津田宏治, 梅津光央

    化学工学会年会研究発表講演要旨集(CD-ROM) 84th 2019

  11. ライブラリーデザインサイクルによる臨床試験と動物実験を結ぶための種交差性抗体の作製

    服部修平, 服部峰充, 本田亜由美, 二井手哲平, 中澤光, 山口純奈, 西裕志, 梅津光央

    日本細胞生物学会大会(Web) 71st 2019

  12. AIが導くタンパク質の進化:指向性が強い変異体は必要か?

    及川未早来, 齋藤裕, 齋藤裕, 亀田倫史, 亀田倫史, 中澤光, 二井手哲平, 津田宏治, 津田宏治, 梅津光央, 梅津光央

    日本細胞生物学会大会(Web) 71st 2019

  13. 抗体の配列柔軟性を利用した部分構造移植による機能性タンパク質の創出

    阿久津澪, 中澤光, 二井手哲平, 亀田倫史, 宮田健, 梅津光央

    日本生物工学会大会講演要旨集 71st 2019

  14. AIを利用したスマートホットライブラリーデザイン:AIはGFPをYFP化できるか?

    及川未早来, 中澤光, 二井手哲平, 亀田倫史, 齋藤裕, 津田宏治, 津田宏治, 梅津光央, 梅津光央

    日本蛋白質科学会年会プログラム・要旨集 18th 2018

  15. 抗体移植を意識したβ-ヘアピン構造足場を利用した分子標的ペプチド取得

    菊地真裕, 二井手哲平, 中澤光, 今中洋行, 梅津光央

    日本生物工学会大会講演要旨集 70th 2018

  16. AIはタンパク質進化を導くか?:機械学習支援によるGFPのYFP化検証

    及川未早来, 齋藤裕, 亀田倫史, 中澤光, 二井手哲平, 津田宏治, 津田宏治, 梅津光央, 梅津光央

    日本生物工学会大会講演要旨集 70th 2018

  17. データベースからの小規模繰り返しライブラリー設計による抗体断片の発現向上

    服部修平, 本田亜由美, 二井手哲平, 中澤光, 梅津光央

    化学工学会秋季大会研究発表講演要旨集(CD-ROM) 50th 2018

  18. 終止コドンを除去したライブラリーを使った生体外選択法

    伊藤智之, 西羽美, 亀田倫史, 二井手哲平, 中澤光, 梅津光央

    日本蛋白質科学会年会プログラム・要旨集 18th 2018

  19. β-ヘアピン構造に着目したペプチド医薬と抗体医薬の同時開発

    菊地真裕, 二井手哲平, 中澤光, 今中洋行, 梅津光央

    日本蛋白質科学会年会プログラム・要旨集 18th 2018

  20. ドライとウェットの両側面からの抗体に代わる分子標的足場タンパク質の検討

    伊藤智之, 西羽美, 亀田倫史, 二井手哲平, 中澤光, 梅津光央

    日本生物工学会大会講演要旨集 70th 2018

  21. 低分子医薬候補分子の親和性向上を目指した薬剤修飾ペプチド提示ファージライブラリーの可能性

    高橋拓人, 二井手哲平, 中澤光, 今中洋行, 梅津光央

    日本蛋白質科学会年会プログラム・要旨集 18th 2018

  22. 光に応答して活性化するハイブリッド酵素デザイン

    中澤光, 石垣友理, 二井手哲平, 梅津光央

    酵素工学研究会講演会講演要旨集 80th 2018

  23. ファージ提示法とドメインライブラリー発想を連結した高活性T-cell recruiting抗体の迅速創出

    杉山在生人, 中澤光, 村上明一, 岸本英博, 梅津光央

    日本分子生物学会年会プログラム・要旨集(Web) 41st 2018

  24. 進化工学的操作と高速傷害活性評価システムを組み合わせた高活性T-cell recruiting抗体の迅速創出

    杉山在生人, 中澤光, 村上明一, 岸本英博, 梅津光央

    化学工学会秋季大会研究発表講演要旨集(CD-ROM) 50th 2018

  25. 親和性ペプチド分子による有機結晶の構造制御と生体分子-半導体有機結晶ハイブリッド材料作製プロセスの開発 (特集 創造的プロセス開発の新展開)

    二井手 哲平, 中澤 光, 梅津 光央

    ケミカルエンジニヤリング = Chemical engineering 62 (7) 483-487 2017/07

    Publisher: 化学工業社

    ISSN: 0387-1037

  26. 繰り返し飽和変異法の確実性を高める迅速な変異体群の作製と機能評価プロセスの開発

    及川未早来, 中澤光, 二井手哲平, 亀田倫史, 齋藤裕, 津田宏治, 津田宏治, 梅津光央, 梅津光央

    日本蛋白質科学会年会プログラム・要旨集 17th 2017

  27. 段階的変異導入による効率的な指向的進化工学手法の構築

    菊池沙也香, 服部峰充, 中澤光, 二井手哲平, 梅津光央

    日本生化学会大会(Web) 90th 2017

  28. 低分子医薬の欠点を補完する有機低分子修飾ペプチドフォーマットの可能性

    高橋拓人, 二井手哲平, 中澤光, 今中洋行, 梅津光央

    日本蛋白質科学会年会プログラム・要旨集 17th 2017

  29. 配列相同性を利用した難発現低分子抗体の発現量向上

    服部修平, 熊谷維子, 中澤光, 二井手哲平, 金子美華, 加藤幸成, 梅津光央

    日本蛋白質科学会年会プログラム・要旨集 17th 2017

  30. 抗体データベースを利用した大規模変異導入による難発現抗体断片の発現量向上プロセスの提案

    服部修平, 二井手哲平, 中澤光, 本田亜由美, 梅津光央

    日本生物工学会大会講演要旨集 69th 2017

  31. 核酸医薬のDDSに利用可能な低分子抗体の設計

    三浦大輔, 服部峰充, 二井手哲平, 中澤光, 梅津光央

    日本生化学会大会(Web) 90th 2017

  32. 飽和変異法とライブラリー的手法の融合による効率的な指向的進化工学の提案

    菊池沙也香, 服部峰充, 中澤光, 二井手哲平, 梅津光央

    日本蛋白質科学会年会プログラム・要旨集 17th 2017

  33. 抗体断片の発現量向上を目的とした抗体データベースによる大規模変異導入プロセスの提案

    服部修平, 本田亜由美, 二井手哲平, 中澤光, 梅津光央

    化学工学会秋季大会研究発表講演要旨集(CD-ROM) 49th 2017

  34. タンパク質の機能改変を効率化するライブラリーデザインサイクルの提案

    菊池沙也香, 服部峰充, 中澤光, 二井手哲平, 梅津光央

    日本生物工学会大会講演要旨集 69th 2017

  35. 終止コドンを排除したライブラリー設計によるループペプチド開発

    菊地真裕, 二井手哲平, 中澤光, 今中洋行, 梅津光央

    日本蛋白質科学会年会プログラム・要旨集 17th 2017

  36. Contact orderから見た組換えタンパク質の物性相関

    伊藤智之, 西羽美, 亀田倫史, 二井手哲平, 中澤光, 梅津光央

    日本蛋白質科学会年会プログラム・要旨集 17th 2017

  37. 二重特異性材料認識抗体によるナノ材料の集積化

    二井手哲平, 真鍋法義, 中澤光, 熊谷泉, 梅津光央

    日本蛋白質科学会年会プログラム・要旨集 17th 2017

  38. Combination of molecular evolution and conformational information for antibody mimic

    梅津光央, 中澤光, 二井手哲平

    Medchem News (Web) 27 (1) 2017

    ISSN: 2432-8626

  39. 低分子抗体-薬物複合体開発:リジン残基側鎖の化学反応へ界面活性剤が及ぼす影響

    服部修平, 服部峰充, 中澤光, 二井手哲平, 松永淳, LEE Seon Hwa, 大江知行, 梅津光央

    日本生物工学会大会講演要旨集 68th 2016

  40. ファージ提示法を利用したCDR模倣ペプチドライブラリーの構築

    柳沢美貴, 二井手哲平, 服部峰充, 中澤光, 熊谷泉, 梅津光央

    日本生物工学会大会講演要旨集 68th 2016

  41. 難発現抗体断片を大腸菌発現させるデータベース利用

    服部修平, 齋琢磨, 服部峰充, 中澤光, 二井手哲平, 亀田倫史, 熊谷維子, 金子美華, 加藤幸成, 梅津光央

    日本分子生物学会年会プログラム・要旨集(Web) 39th 2016

  42. 蛋白質の分子認識を利用したプラズモニック膜と多孔質膜のボトムアップ作製プロセス

    二井手哲平, 真鍋法義, 中澤光, 服部峰充, 熊谷泉, 梅津光央

    化学工学会大会講演要旨集(CD-ROM) 2015 2015

  43. 1P-283 Biomass-binding peptides designed by molecular evolution for efficient degradation of cellulose in biomass by cellulase

    Nakazawa Hikaru, Ishigaki Yuri, Ikeuchi Akinori, Kouda Katsunori, Yasutani Noriko, Onishi Toru, Umetsu Mitsuo

    67 159-159 2015

    Publisher: 日本生物工学会

  44. 2P-055 Domain library approach describes rules for highly cytotoxic antibody

    Sugiyama Aruto, Umetsu Mitsuo, Nakazawa Hikaru, Asano Ryutaro, Kumagai Izumi

    67 188-188 2015

    Publisher: 日本生物工学会

  45. 2P-051 Development of an artificial cellulase utilizing cellulose-binding DNA aptamer

    Takahara Mari, Mori Yutaro, Budinova Geisa A.L.G., Nakazawa Hikaru, Umetsu Mitsuo, Kamiya Noriho

    67 187-187 2015

    Publisher: 日本生物工学会

  46. 2P-056 Influence of amino acid sequence homology on dimerization of diabody-type

    Onodera Tomoko, Umetsu Mitsuo, Tanaka Yoshikazu, Nakazawa Hikaru, Hattori takamitsu, Asano Ryutaro, Kumagai Izumi

    67 188-188 2015

    Publisher: 日本生物工学会

  47. 3P-036 How effective new small bispecific antibodies are created from existing antibody library

    Sugiyama Aruto, Nakazawa Hikaru, Hosokawa Katsuhiro, Asano Ryutaro, Kumagai Izumi, Umetsu Mitsuo

    66 203-203 2014

    Publisher: 日本生物工学会

  48. 2P-057 Synergistic effect on catalytic activity of cellulase with a number of hybrid nano-cellulosomes designed from library-selected cellulose binding domains

    Nakazawa Hikaru, Okada Izumi, Ishigaki Yuri, Kobayashi Eiko, Umetsu Mitsuo

    66 121-121 2014

    Publisher: 日本生物工学会

  49. 2P-058 Kimera cellulase design from module library approach

    Okada Izumi, Nakazawa Hikaru, Ishigaki Yuri, Kobayashi Eiko, Umetsu Mitsuo

    66 121-121 2014

    Publisher: 日本生物工学会

  50. 2P-083 High performance artificial cellulosome design based on protein module library on nanomaterial

    Nakazawa Hikaru, Ishigaki Yuri, Kumagai Izumi, Umetsu Mitsuo

    65 124-124 2013

    Publisher: 日本生物工学会

  51. 酸化亜鉛コーティングプラズモニックチップ上のサンドイッチアッセイによるうつ病関連マーカーBDNFの迅速検出

    佐藤茉莉, 佐藤茉莉, 田和圭子, 上垣浩一, 原とも子, 梅津光央, 中澤光, 熊谷泉, 板倉誠, 板倉誠, 高橋正身, 高橋正身, 青田浩幸, 小島正己, 小島正己

    高分子学会予稿集(CD-ROM) 62 (1) 2013

  52. Ca1-2 セルロース系バイオマス分解におけるTrichoderma reeseiヘミセルラーゼの役割(セルラーゼおよび関連酵素,一般講演,日本応用糖質科学会平成24年度大会(第61回))

    齋藤 勇司, 長野 まどか, 三井 勇輔, 小松 光子, 中澤 光, 小笠原 渉, 森川 康, 二階堂 満, 戸谷 一英, 岡田 宏文

    応用糖質科学 : 日本応用糖質科学会誌 2 (3) B39 2012/08/20

    Publisher: 日本応用糖質科学会

    ISSN: 2185-6427

  53. Ca1-1 Trichoderma reesei CBH IIの親水性がバイオマス糖化に及ぼす影響(セルラーゼおよび関連酵素,一般講演,日本応用糖質科学会平成24年度大会(第61回))

    小松 光子, 齋藤 勇司, 中澤 光, 二階堂 満, 戸谷 一英, 小笠原 渉, 森川 康, 岡田 宏文

    応用糖質科学 : 日本応用糖質科学会誌 2 (3) B38 2012/08/20

    Publisher: 日本応用糖質科学会

    ISSN: 2185-6427

  54. 4Ca15 Hybrid nanocellulosome: Nanocluster design of high performancve cellulases with multivalent cellulose-binding modules

    Nakazawa Hikaru, Kim Do-myoung, Matsuyama Takashi, Ishida Nobuhiro, Ikeuchi Akinori, Kumagai Izumi, Umetsu Mitsuo

    64 195-195 2012

    Publisher: 日本生物工学会

  55. うつ病候補マーカーであるBDNFの酸化亜鉛コーティングプラズモニックチップを用いた迅速・高感度検出

    佐藤茉莉, 田和圭子, 上垣浩一, 原とも子, 梅津光央, 中澤光, 熊谷泉, 青田浩幸, 松本昭, 小島正己

    日本化学会講演予稿集 92nd (1) 2012

    ISSN: 0285-7626

  56. 4Ia09 Role of endoglucanase I and II from Trichoderma reesei in biomass degradation

    Mitsui Yusuke, Saito Yuji, Nagano Madoka, Komatsu Mitsuko, Nakazawa Hikaru, Ogasawara Wataru, Morikawa Yasushi, Okada Hirofumi, Totani Kazuhide, Nikaido Mitsuru

    64 241-241 2012

    Publisher: 日本生物工学会

  57. 3P-1050 Characterization of two endoglucanases from Lumbricus rubellus and saccharification of biomass

    AKAZAWA Shin-ichi, IKARASHI Yuki, YARIMIZU Jun, YOKOYAMA Daichi, NAKAZAWA Hikaru, MORIKAWA Yasushi, OGASAWARA Wataru

    22 70-70 2010

    Publisher: 日本生物工学会

  58. 2Da09 Analysis of polysaccharide-degrading enzymes from Lumbricus rubellus

    AKAZAWA Shin-ichi, YARIMIZU Jun, NAKAZAWA Hikaru, OGASAWARA Wataru, MORIKAWA Yasushi

    21 45-45 2009

    Publisher: 日本生物工学会

  59. 3Ga10 Disaccharide-condensing activity of Trichoderma reesei EG I catalytic domain

    TOTANI Kazuhide, YOSHIDA Naoki, NAKAZAWA Hikaru, OGASAWARA Wataru, OKADA Hirofumi, MORIKAWA Yasushi

    20 187-187 2008

    Publisher: 日本生物工学会

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Books and Other Publications 6

  1. 微生物を活用した有用物質の製造技術

    中澤 光、梅津 光央

    シーエムシー出版 2023/05

    ISBN: 9784781317403

  2. 生物工学会誌 バイオミディア 酵素はメカ化できるのか?

    中澤 光

    生物工学会 2019/04

  3. MEDCHEM NEWS

    Mitsuo Umetsu, Hikaru Nakazawa, Teppei Niide

    2017/02/01

  4. ケミカルエンジニヤリング 親和性ペプチド分子による有機結晶の構造制御と生体分子-半導体有機結晶ハイブリッド材料作製プロセスの開発

    二井手哲平, 中澤 光, 梅津光央

    化学工業社 2017/01

  5. 進化分子工学

    梅津 光央, 中澤 光, 服部 峰充

    エヌティー・エス 2013

  6. バイオマス分解関連酵素研究の最前線

    梅津 光央, 金 渡明, 中澤 光

    シーエムシー出版 2012

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Presentations 7

  1. Machine learning-assisted molecular evolution for stable enzyme engineering Invited

    Hikaru Nakazawa

    25th NEA symposium Synthetic Biology 2024 2024/09/10

  2. タンパク質の自動設計は可能になるのか?:ドメインライブラリアプローチと機械学習支援 Invited

    中澤 光

    日本化学会 バイオ関連化学若手フォーラム 2019/09/03

  3. 蛋白質機能を向上するためのドメインライブラリー設計 Invited

    中澤 光

    日本化学会 東北支部会 2019/07/12

  4. 分子認識アプタマー開発における進化分子工学操作の新しい展開 Invited

    中澤 光, 梅津光央

    日本分析化学会第79回分析化学討論会マイクロ・ナノで生命を測る 2019/05/14

  5. 共役効果を意識したモジュールライブラリー発想人工セルロソーム設計 Invited

    中澤 光, 石垣友理, 岡田 和, 小林栄子, 梅津光央

    第29回 セルラーゼ研究会 2015/07/17

  6. モジュールライブラリーという発想からの進化工学的人工セルロソーム設計 Invited

    中澤 光, 石垣友理, 岡田 和, 小林栄子, 梅津光央

    第28回セルラーゼ研究会 2014/07/11

  7. 酵素共役系を意識したモジュール集積によるハイブリッドセルロソームの設計 Invited

    中澤 光, 金 渡明, 熊谷 泉, 梅津 光央

    新学術領域融合マテリアル:分子制御による材料創成と機能開拓, 第五回若手スクール 2012/11/26

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Industrial Property Rights 7

  1. 糖化残差成分結合能を有するペプチドおよびその利用

    Property Type: Patent

  2. セルロース系バイオマスからの糖およびアルコールの製造方法

    5745237号

    Property Type: Patent

  3. ダイアボディ型BsAbを発現・分泌するビフィドバクテリウム属細菌

    嶋谷裕子, 小林聡, 塩谷公一郎, 片岡之郎, 関雄史, 松村富穂, 金成安慶, 梅津光央, 中澤 光

    Property Type: Patent

  4. プラスミド一周PCR法を用いたランダム遺伝子プラスミドライブラリー作成方法、それを用いた形質転換体作成方法、および、その方法に使用するキット

    中澤 光, 柳沢美貴, 二井手哲平, 服部峰充, 梅津光央

    Property Type: Patent

  5. 抗体断片及び該抗体を含む二重特異性抗体

    梅津光央, 杉山在生人, 中澤 光, 二井手哲平, 岸本英博, 村上明一

    Property Type: Patent

  6. 標的分子と結合するポリペプチド

    梅津光央, 伊藤智之, 西羽美, 中澤 光, 二井手哲平, 亀田倫史

    Property Type: Patent

  7. セルロース系バイオマスからの糖及びアルコールの製造方法、並びに該方法に 用いられる微生物

    中澤 光, 小笠原渉, 岡田宏文, 森川康, 小林良則, 川口剛司, 炭谷順一, 谷 修治

    Property Type: Patent

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Research Projects 7

  1. 機械学習×進化工学が指し示すタンパク質のif進化:創薬酵素の高度成熟・機能化

    梅津 光央, 中澤 光, 伊藤 智之, 田中 良和

    Offer Organization: 日本学術振興会

    System: 科学研究費助成事業

    Category: 基盤研究(B)

    Institution: 東北大学

    2024/04/01 - 2027/03/31

  2. 精密移植&フィッティング技術により挑戦する金属表面滑走モータータンパク質創出

    中澤 光

    Offer Organization: 日本学術振興会

    System: 科学研究費助成事業

    Category: 挑戦的研究(萌芽)

    Institution: 東北大学

    2022/06/30 - 2025/03/31

    More details Close

    キネシンはモータータンパク質として知られており、「走る」という動的性質からナノスケールのアクチュエーターとして期待されており、最近ではアメーバ状ナノロボットや繊維状ナノロボットの駆動力として使われている。キネシンのマイクロチューブリン上しか移動できないという使用の制限を解決するために、本申請は、マイクロチューブリン表面以外の無機材料表面を走るキネシンタンパク質の開発に挑戦した。キネシンは、ループL11とループL12によって微小管の表面に繰り返し存在するそれぞれの相互作用部分とATP依存で交互に結合することによって、走っていることがわかってきた。結合は物理吸着であることから、申請者は「走る」ためには、キネシンの動く相互作用部位と、結合対象の「8nm」の幅で繰り返す相互作用部位が重要と考えた。本申請では①キネシンの相互作用ループへの結合ペプチドの移植および②相互作用部位を一定の間隔で配置したナノマテリアル構造体の作製を行い、無機材料表面を走るキネシンタンパク質の開発にチャレンジする。 当該年度はC末端ビオチン化したNeurospora Crassa 由来のキネシンをすでに大腸菌を宿主として大量発現させていたが、調製に難航した。大腸菌にてより発現量の多いキネシンが見つかったためそれを用いた方が今後の実験が円滑に進むと考え、新たに、タグ融合遺伝子構築を行った。このキネシンを用いて所属する研究室でペプチド移植を進めていくこととする。移植に関してはまだ行っていないが、予定通り金結合ペプチドおよび酸化亜鉛結合ペプチド)の長さを調節し、キネシンのループL11とループL12それぞれに移植、あるいはシリカ結合ペプチドを両ループに移植することを想定して遺伝子を設計した。

  3. 光-動力変換ナノデバイスの動作原理に関する予備検討

    Offer Organization: 国立研究開発法人科学技術振興機構(JST)

    System: 戦略的創造研究推進事業(さきがけ「光融合」)特定課題調査

    Category: 戦略的創造研究推進事業(さきがけ「光融合」)特定課題調査

    Institution: 東北大学

    2024/10 - 2025/03

  4. 光照射で酵素の活性を向上するスキャフォ―ルド粉体の開発

    Offer Organization: ホソカワ粉体工学振興財団

    System: 研究助成

    Category: 研究助成

    Institution: 東北大学

    2021/04 - 2022/03

  5. Nanobio antifungal agent for fungal pandemics

    NAKAZAWA HIKARU

    Offer Organization: Japan Society for the Promotion of Science

    System: Grants-in-Aid for Scientific Research

    Category: Grant-in-Aid for Scientific Research (C)

    Institution: Tohoku University

    2018/04/01 - 2021/03/31

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    Japanese mold (Candida aureas) has become poisonous overseas, causing the first mycotic pandemic (global epidemic) in Europe, the United States and Asia.The development of antifungal agents with a new mechanism of action that is difficult to have resistance is expected.In this study, we have developed a nanobio antifungal agent that exhibits antifungal activity by using the natural antifungal enzyme chitinase on the surface of silver nanoparticles that have high antifungal activity and are less likely to develop resistance.

  6. An artificial enzyme for improvement of enzymatic activity by irradiation of sun light.

    Nakazawa Hikaru

    Offer Organization: Japan Society for the Promotion of Science

    System: Grants-in-Aid for Scientific Research Grant-in-Aid for Young Scientists (B)

    Category: Grant-in-Aid for Young Scientists (B)

    Institution: Tohoku University

    2016/04/01 - 2019/03/31

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    Non-edible biomass expected and its convert to energy and chemicals. In case of use of rigid cellulose. It is necessary to degrade for long period. Enzymatic activity should be enhanced naturally without heat source like boiler. Here, we constructed novel enzyme design for eco-carbon cycles by use of star shape gold nanoparticles with conversion of sun light to heat. Consequently, clustering effect of cellulase module on the surface of nanoparticle and enhanced reaction activity in nanoparticle surface by Light-heat effect of Gold nanostar result in 5 times increase in saccharification activity of cellulase module.

  7. Application of hybrid nano-assembly for in-vitro synthetic biology tool

    Umetsu Mitsuo

    Offer Organization: Japan Society for the Promotion of Science

    System: Grants-in-Aid for Scientific Research Grant-in-Aid for Scientific Research (B)

    Category: Grant-in-Aid for Scientific Research (B)

    Institution: Tohoku University

    2016/04 - 2019/03

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    In vivo, a series of enzymes are closely packed in a minute space, and the enzyme reactions are coupled. In this study, enzymes are clustered on nanoparticles and the clustered enzymes are hierarchically assembled to reconstruct in-vivo-mimic enzyme-crowded environment. The utilization of material-binding peptides and proteins showed the possibility for spontaneous self-assembly of clustered enzymes.

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Teaching Experience 5

  1. Molecular Biological Engineering Tohoku University

  2. Chemical and Biomolecular Engineering II Tohoku University

  3. Biofunctional Chemistry Tohoku University

  4. Life Sciences B Tohoku University

  5. Exercises B Tohoku University

Social Activities 1

  1. タンパク質の進化分子工学×AIでバイオ医薬品の開発

    地域創造学

    2024/11/05 - Present