Updated on 2022/03/31

写真a

 
HAYASHI Gosuke
 
Organization
Graduate School of Engineering Biomolecular Engineering 1 Associate professor
Graduate School
Graduate School of Engineering
Undergraduate School
School of Engineering Chemistry and Biotechnology
Title
Associate professor
Contact information
メールアドレス
External link

Degree 1

  1. 博士(理学) ( 2009.3   大阪大学 ) 

Research Interests 3

  1. Peptide chemistry

  2. Chemical protein synthesis

  3. Epigenetics

Research Areas 3

  1. Nanotechnology/Materials / Bio chemistry

  2. Nanotechnology/Materials / Chemistry and chemical methodology of biomolecules

  3. Nanotechnology/Materials / Bio chemistry

Research History 13

  1. Nagoya University   Graduate School of Engineering, Department of Bimolecular Engineering   Associate professor

    2019.3

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    Country:Japan

  2. Nagoya University   Graduate School of Engineering, Department of Bimolecular Engineering   Associate professor

    2019.3

  3. Nagoya University   Graduate School of Engineering Biomolecular Engineering 1   Associate professor

    2019.3

  4. The University of Tokyo   Graduate School of Engineering, Department of Chemistry and Biotechnology   Assistant Professor

    2013.2 - 2019.2

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    Country:Japan

  5. The University of Tokyo   Graduate School of Engineering, Department of Chemistry and Biotechnology   Assistant Professor

    2013.2 - 2019.2

  6. The University of Tokyo   Research Center for Advanced Science and Technology   Assistant Professor

    2012.6 - 2013.1

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    Country:Japan

  7. The University of Tokyo   Research Center for Advanced Science and Technology   Designated assistant professor

    2012.6 - 2013.1

  8. Boston University   Department of Biomedical Engineering   Postdoctral Fellow (JSPS Reserch Fellowship for Young Scientists PD and Overseas Research Fellowships)

    2011.2 - 2012.5

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    Country:Japan

  9. Boston University   Department of Biomedical Engineering   Postdoctral Fellow (JSPS Reserch Fellowship for Young Scientists PD and Overseas Research Fellowships)

    2011.2 - 2012.5

  10. The University of Tokyo   Research Center for Advanced Science and Technology   Postdoctral Fellow (JSPS Research Fellowship for Young Scientists PD)

    2009.4 - 2011.2

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    Country:Japan

  11. The University of Tokyo   Research Center for Advanced Science and Technology   Postdoctral Fellow (JSPS Research Fellowship for Young Scientists PD)

    2009.4 - 2011.2

  12. Osaka University   Graduate School of Science, Department of Chemistry   JSPS Research Fellowship of Young Scientists DC1

    2006.4 - 2009.3

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    Country:Japan

  13. Osaka University   Graduate School of Science, Department of Chemistry   JSPS Research Fellowship of Young Scientists DC1

    2006.4 - 2009.3

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Education 6

  1. Osaka University   Graduate School, Division of Natural Science   Department of Chemistry

    2006.4 - 2009.3

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    Country: Japan

  2. Osaka University   Graduate School, Division of Natural Science   Department of Chemistry

    2006.4 - 2009.3

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    Country: Japan

  3. Kyoto University   Graduate School, Division of Engineering   Department of Synthetic Chemistry and Biological Chemistry

    2004.4 - 2006.3

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    Country: Japan

  4. Kyoto University   Graduate School, Division of Engineering   Department of Synthetic Chemistry and Biological Chemistry

    2004.4 - 2006.3

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    Country: Japan

  5. Kyoto University   Faculty of Engineering   Undergraduate School of Industrial Chemistry

    2000.4 - 2004.3

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    Country: Japan

  6. Kyoto University   Faculty of Engineering   Undergraduate School of Industrial Chemistry

    2000.4 - 2004.3

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    Country: Japan

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Professional Memberships 10

  1. 日本化学会

  2. 日本生化学会

  3. 日本分子生物学会

  4. 日本ケミカルバイオロジー学会

  5. 日本エピジェネティクス研究会

  6. 日本生化学会

  7. 日本化学会

  8. 日本分子生物学会

  9. 日本ケミカルバイオロジー学会

  10. 日本エピジェネティクス研究会

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Awards 14

  1. 若い世代の特別講演賞

    2020.3   日本化学会  

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    Award type:Award from Japanese society, conference, symposium, etc.  Country:Japan

  2. 若い世代の特別講演賞

    2020.3   日本化学会  

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    Award type:Award from international society, conference, symposium, etc.  Country:Japan

  3. 日本ペプチド学会 奨励賞

    2019.11   日本ペプチド学会  

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    Award type:Award from Japanese society, conference, symposium, etc.  Country:Japan

  4. 日本ペプチド学会 奨励賞

    2019.11   日本ペプチド学会  

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    Award type:Award from international society, conference, symposium, etc.  Country:Japan

  5. 日本エピジェネティクス研究会 奨励賞

    2018.3   日本エピジェネティクス研究会  

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    Award type:Award from Japanese society, conference, symposium, etc.  Country:Japan

  6. 日本エピジェネティクス研究会 奨励賞

    2018.3   日本エピジェネティクス研究会  

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    Award type:Award from international society, conference, symposium, etc.  Country:Japan

  7. バイオ関連化学シンポジウム 講演賞

    2017.9   日本化学会  生体機能関連化学部会、バイオテクノロジー部会  

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    Award type:Award from Japanese society, conference, symposium, etc.  Country:Japan

  8. バイオ関連化学シンポジウム 講演賞

    2017.9   日本化学会 生体機能関連化学部会、バイオテクノロジー部会  

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    Award type:Award from international society, conference, symposium, etc.  Country:Japan

  9. 日本化学会優秀講演賞(学術)

    2017.3   日本化学会  

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    Award type:Award from Japanese society, conference, symposium, etc.  Country:Japan

  10. 日本化学会優秀講演賞(学術)

    2017.3   日本化学会  

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    Award type:Award from international society, conference, symposium, etc.  Country:Japan

  11. Outstanding Young Researcher Poster Presentation Award

    2010.12   PACIFICHEM2010  

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    Award type:Award from international society, conference, symposium, etc.  Country:Japan

  12. Outstanding Young Researcher Poster Presentation Award

    2010.12   PACIFICHEM2010  

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    Award type:International academic award (Japan or overseas)  Country:Japan

  13. Poster Award in 4th International Symposium on Nucleic Acids Chemistry

    2005.9   日本核酸化学会  

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    Award type:Award from international society, conference, symposium, etc.  Country:Japan

  14. Poster Award in 4th International Symposium on Nucleic Acids Chemistry

    2005.9   日本核酸化学会  

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    Award type:International academic award (Japan or overseas)  Country:Japan

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Papers 53

  1. Monobodies with potent neutralizing activity against SARS-CoV-2 Delta and other variants of concern

    Kondo Taishi, Matsuoka Kazuhiro, Umemoto Shun, Fujino Tomoshige, Hayashi Gosuke, Iwatani Yasumasa, Murakami Hiroshi

    LIFE SCIENCE ALLIANCE   Vol. 5 ( 6 )   2022.6

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    Language:Japanese   Publishing type:Research paper (scientific journal)   Publisher:Life science alliance  

    Neutralizing antibodies against the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) are useful for patients' treatment of the coronavirus disease 2019 (COVID-19). We report here affinity maturation of monobodies against the SARS-CoV-2 spike protein and their neutralizing activity against SARS-CoV-2 B.1.1 (Pango v.3.1.14) as well as four variants of concern. We selected matured monobodies from libraries with multi-site saturation mutagenesis on the recognition loops through in vitro selection. One clone, the C4-AM2 monobody, showed extremely high affinity (KD < 0.01 nM) against the receptor-binding domain of the SARS-CoV-2 B.1.1, even in monomer form. Furthermore, the C4-AM2 monobody efficiently neutralized the SARS-CoV-2 B.1.1 (IC50 = 46 pM, 0.62 ng/ml), and the Alpha (IC50 = 77 pM, 1.0 ng/ml), Beta (IC50 = 0.54 nM, 7.2 ng/ml), Gamma (IC50 = 0.55 nM, 7.4 ng/ml), and Delta (IC50 = 0.59 nM, 8.0 ng/ml) variants. The obtained monobodies would be useful as neutralizing proteins against current and potentially hazardous future SARS-CoV-2 variants.

    DOI: 10.26508/lsa.202101322

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  2. Construction of a Highly Diverse mRNA Library for in vitro Selection of Monobodies

    Kondo Taishi, Eguchi Minori, Tsuzuki Nariaki, Murata Naoya, Fujino Tomoshige, Hayashi Gosuke, Murakami Hiroshi

    BIO-PROTOCOL   Vol. 11 ( 16 ) page: e4125   2021.8

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    Language:Japanese   Publishing type:Research paper (scientific journal)   Publisher:Bio-protocol  

    Recently, we developed transcription/translation coupled with the association of puromycin linker (TRAP) display as a quick in vitro selection method to obtain antibody-like proteins. For the in vitro selection, it is important to prepare mRNA libraries among which the diversity is high. Here, we describe a method for the preparation of monobody mRNA libraries with greater than 1013 theoretical diversity. First, we synthesized two long single-stranded DNAs that corresponded to fragments of monobody DNA, with random codons in the BC and FG loops. These oligonucleotides were ligated by T4 DNA ligase with the support of guide oligonucleotides containing 3′ ends that were protected by a modification. After amplifying the product DNAs by PCR, one end of each DNA fragment was digested with the type II restriction enzyme BsaI, and the resulting DNA fragments were ligated using T4 DNA ligase. After amplification of the DNA product, mRNAs were synthesized by T7 RNA polymerase. This method is simple and could be used for the preparation of mRNA libraries for various antibody-like proteins.

    DOI: 10.21769/BioProtoc.4125

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  3. Base-resolution analysis of 5-hydroxymethylcytidine by selective oxidation and reverse transcription arrest

    Koyama Kenta, Hayashi Gosuke, Ueda Hiroki, Ota Satoshi, Nagae Genta, Aburatani Hiroyuki, Okamoto Akimitsu

    ORGANIC & BIOMOLECULAR CHEMISTRY   Vol. 19 ( 29 ) page: 6478 - 6486   2021.8

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    Language:Japanese   Publishing type:Research paper (scientific journal)   Publisher:Organic and Biomolecular Chemistry  

    While 5-hydroxymethylcytidine in RNA (hm5C) is associated with cellular development and differentiation, its distribution and biological function remain largely unexplored because suitable detection methods are lacking. Here, we report a base-resolution sequencing method forhm5C in RNA by applying peroxotungstate-mediated chemical conversion ofhm5C to trihydroxylated thymine (thT). Reverse transcription by SuperScript III terminated at thethT site, probably because of its unnatural nucleobase structure producing truncated cDNA. Consequently, base-resolution analysis of thehm5C sites in RNA was achieved with both Sanger sequencing and Illumina sequencing analysis by comparing sequencing data before and after peroxotungstate treatment.

    DOI: 10.1039/d1ob00995h

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  4. Silyl-protected propargyl glycine for multiple labeling of peptides by chemoselective silyl-deprotection

    Kamo Naoki, Hayashi Gosuke, Okamoto Akimitsu

    TETRAHEDRON LETTERS   Vol. 73   2021.6

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    Language:Japanese   Publishing type:Research paper (scientific journal)   Publisher:Tetrahedron Letters  

    We synthesized Fmoc-propargyl glycine derivatives bearing different silyl protecting groups that can be readily introduced by using a standard solid-phase peptide coupling procedures. Taking advantage of the orthogonality between the different silyl protecting groups, chemoselective incorporation of functional molecules into a 19-mer peptide through click reactions was demonstrated.

    DOI: 10.1016/j.tetlet.2021.153093

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  5. Organoruthenium-catalyzed chemical protein synthesis to elucidate the functions of epigenetic modifications on heterochromatin factors

    Kamo Naoki, Kujirai Tomoya, Kurumizaka Hitoshi, Murakami Hiroshi, Hayashi Gosuke, Okamoto Akimitsu

    CHEMICAL SCIENCE   Vol. 12 ( 16 ) page: 5926 - 5937   2021.4

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    Language:Japanese   Publishing type:Research paper (scientific journal)   Publisher:Chemical Science  

    The application of organometallic compounds for protein science has received attention. Recently, total chemical protein synthesis using transition metal complexes has been developed to produce various proteins bearing site-specific posttranslational modifications (PTMs). However, in general, significant amounts of metal complexes were required to achieve chemical reactions of proteins bearing a large number of nucleophilic functional groups. Moreover, syntheses of medium-size proteins (>20 kDa) were plagued by time-consuming procedures due to cumbersome purification and isolation steps, which prevented access to variously decorated proteins. Here, we report a one-pot multiple peptide ligation strategy assisted by an air-tolerant organoruthenium catalyst that showed more than 50-fold activity over previous palladium complexes, leading to rapid and quantitative deprotection on a protein with a catalytic amount (20 mol%) of the metal complex even in the presence of excess thiol moieties. Utilizing the organoruthenium catalyst, heterochromatin factors above 20 kDa, such as linker histone H1.2 and heterochromatin protein 1α (HP1α), bearing site-specific PTMs including phosphorylation, ubiquitination, citrullination, and acetylation have been synthesized. The biochemical assays using synthetic proteins revealed that the citrullination at R53 in H1.2 resulted in the reduced electrostatic interaction with DNA and the reduced binding affinity to nucleosomes. Furthermore, we identified a key phosphorylation region in HP1α to control its DNA-binding ability. The ruthenium chemistry developed here will facilitate the preparation of a variety of biologically and medically significant proteins containing PTMs and non-natural amino acids.

    DOI: 10.1039/d1sc00731a

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  6. cDNA TRAP display for rapid and stable in vitro selection of antibody-like proteins

    Kondo Taishi, Eguchi Minori, Kito Seita, Fujino Tomoshige, Hayashi Gosuke, Murakami Hiroshi

    CHEMICAL COMMUNICATIONS   Vol. 57 ( 19 ) page: 2416 - 2419   2021.3

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    Language:Japanese   Publishing type:Research paper (scientific journal)   Publisher:Chemical Communications  

    We developed a cDNA TRAP display for the rapid selection of antibody-like proteins in various conditions. By modifying the original puromycin linker in the TRAP display, a monobody was covalently attached to the cDNA. As a proof-of-concept, we demonstrated a rapid model selection of an anti-EGFR1 monobody in a solution containing ribonuclease.

    DOI: 10.1039/d0cc07541h

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  7. Acetylation-modulated communication between the H3 N-terminal tail domain and the intrinsically disordered H1 C-terminal domain

    Hao Fanfan, Murphy Kevin J., Kujirai Tomoya, Kamo Naoki, Kato Junko, Koyama Masako, Okamato Akimitsu, Hayashi Gosuke, Kurumizaka Hitoshi, Hayes Jeffrey J.

    NUCLEIC ACIDS RESEARCH   Vol. 48 ( 20 ) page: 11510 - 11520   2020.11

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    Language:Japanese   Publishing type:Research paper (scientific journal)   Publisher:Nucleic Acids Research  

    Linker histones (H1s) are key structural components of the chromatin of higher eukaryotes. However, the mechanisms by which the intrinsically disordered linker histone carboxy-terminal domain (H1 CTD) influences chromatin structure and gene regulation remain unclear. We previously demonstrated that the CTD of H1.0 undergoes a significant condensation (reduction of end-to-end distance) upon binding to nucleosomes, consistent with a transition to an ordered structure or ensemble of structures. Here, we show that deletion of the H3 N-terminal tail or the installation of acetylation mimics or bona fide acetylation within H3 N-terminal tail alters the condensation of the nucleosome-bound H1 CTD. Additionally, we present evidence that the H3 N-tail influences H1 CTD condensation through direct protein-protein interaction, rather than alterations in linker DNA trajectory. These results support an emerging hypothesis wherein the H1 CTD serves as a nexus for signaling in the nucleosome.

    DOI: 10.1093/nar/gkaa949

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  8. l-DNA-tagged fluorescencein situhybridization for highly sensitive imaging of RNAs in single cells

    Ogata Motoyuki, Hayashi Gosuke, Ichiu Anri, Okamoto Akimitsu

    ORGANIC & BIOMOLECULAR CHEMISTRY   Vol. 18 ( 40 ) page: 8084 - 8088   2020.10

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    Language:Japanese   Publishing type:Research paper (scientific journal)   Publisher:Organic and Biomolecular Chemistry  

    We report an effective fluorescence in situ hybridization strategy, named l-DNA tagged FISH (LT-FISH), for highly sensitive RNA detection in fixed cultured cells. LT-FISH includes two-step hybridization processes with a l-d chimera oligonucleotide probe and a fluorescence-labeled PCR product tethering a l-DNA tag. The degree of fluorescence enhancement, depending on the length of PCR products, was up to 14-fold when the 606 bp product was used. Endogenous mRNA and miRNA in cancer cells were visualized by utilizing this l-DNA-mediated signal amplification technique.

    DOI: 10.1039/d0ob01635g

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  9. Toolbox for chemically synthesized histone proteins.

    Nakatsu K, Hayashi G, Okamoto A

    Current opinion in chemical biology   Vol. 58   page: 10 - 19   2020.10

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    DOI: 10.1016/j.cbpa.2020.04.016

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  10. Antibody-like proteins that capture and neutralize SARS-CoV-2

    Kondo T., Iwatani Y., Matsuoka K., Fujino T., Umemoto S., Yokomaku Y., Ishizaki K., Kito S., Sezaki T., Hayashi G., Murakami H.

    SCIENCE ADVANCES   Vol. 6 ( 42 )   2020.10

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    Language:Japanese   Publishing type:Research paper (scientific journal)   Publisher:Science Advances  

    To combat severe acute respiratory syndrome–related coronavirus 2 (SARS-CoV-2) and any unknown emerging pathogens in the future, the development of a rapid and effective method to generate high-affinity antibodies or antibody-like proteins is of critical importance. We here report high-speed in vitro selection of multiple high-affinity antibody-like proteins against various targets including the SARS-CoV-2 spike protein. The sequences of monobodies against the SARS-CoV-2 spike protein were successfully procured within only 4 days. Furthermore, the obtained monobody efficiently captured SARS-CoV-2 particles from the nasal swab samples of patients and exhibited a high neutralizing activity against SARS-CoV-2 infection (half-maximal inhibitory concentration, 0.5 nanomolar). High-speed in vitro selection of antibody-like proteins is a promising method for rapid development of a detection method for, and of a neutralizing protein against, a virus responsible for an ongoing, and possibly a future, pandemic.

    DOI: 10.1126/sciadv.abd3916

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  11. Fmoc-Compatible and C-terminal-Sequence-Independent Peptide Alkyl Thioester Formation Using Cysteinylprolyl Imide

    Nakatsu Koki, Yanase Masafumi, Hayashi Gosuke, Okamoto Akimitsu

    ORGANIC LETTERS   Vol. 22 ( 12 ) page: 4670 - 4674   2020.6

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    DOI: 10.1021/acs.orglett.0c01450

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  12. Novel Strategies of Peptide Ligation for Accelerating Chemical Protein Synthesis

    Hayashi Gosuke, Okamoto Akimitsu

    JOURNAL OF SYNTHETIC ORGANIC CHEMISTRY JAPAN   Vol. 78 ( 2 ) page: 130 - 139   2020.2

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  13. Novel Strategies of Peptide Ligation for Accelerating Chemical Protein Synthesis

    Hayashi Gosuke, Okamoto Akimitsu

    JOURNAL OF SYNTHETIC ORGANIC CHEMISTRY JAPAN   Vol. 78 ( 2 ) page: 130-139   2020.2

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  14. タンパク質化学合成を活用した翻訳後修飾研究

    林 剛介

    ファルマシア   Vol. 56 ( 1 ) page: 46-50 - 50   2020

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    Language:English   Publishing type:Research paper (scientific journal)   Publisher:公益社団法人 日本薬学会  

    タンパク質化学合成法の発展により、多様な翻訳後修飾を持つタンパク質の作製が可能なってきた。本稿では、タンパク質化学合成法について解説するとともに、化学合成タンパク質を用いた翻訳後修飾研究について紹介する。特に、エピジェネティクス研究で中心的役割を果たすヒストンタンパク質の翻訳後修飾研究、また本特集のテーマであるユビキチン鎖やユビキチン化タンパク質を化学的に合成し、応用した研究例について紹介する。

    DOI: 10.14894/faruawpsj.56.1_46

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  15. Novel Strategies of Peptide Ligation for Accelerating Chemical Protein Synthesis

    Hayashi Gosuke, Okamoto Akimitsu

    Journal of Synthetic Organic Chemistry, Japan   Vol. 78 ( 2 ) page: 130 - 139   2020

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    Language:Japanese   Publishing type:Research paper (scientific journal)   Publisher:The Society of Synthetic Organic Chemistry, Japan  

    <p>Chemical protein synthesis (CPS) that consists of solid-phase peptide synthesis and peptide ligation generates not only naturally-occurring proteins with/without posttranslational modifications (PTMs), but also a variety of artificial proteins including unnatural amino-acids such as ᴅ-amino acids and fluorophore-labeled amino acids. This unique property offers new analytical methods for protein structure and interaction in terms of PTMs. In fact, we have chemically synthesized histone proteins with PTMs, which play an important role in regulation of gene expression in eukaryotic cells, and analyzed the effects of PTMs such as methylation, acetylation, and phosphorylation. However, current CPS is still in developing process and includes several issues to be solved such as difficult handling in hydrophobic protein synthesis and time-consuming multistep process for large protein synthesis. We have approached these issues by creating new strategies for peptide ligation. One-pot ligation of five peptide segments was demonstrated for the first time by utilizing multifunctionality of thiophenol compound in deprotection of allyloxycarbonyl group by palladium complex. New thioester precursors for native chemical ligation, which have potential to offer a novel two-way one-pot ligation, have also been developed recently. Furthermore, we have been developing a new strategy for simultaneous ligation of multiple peptides on DNA scaffold, which can connect peptides in highly diluted condition. This article also describes the background and current situation of CPS with our future perspectives.</p>

    DOI: 10.5059/yukigoseikyokaishi.78.130

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  16. Chemical Synthesis of Cys-Containing Protein via Chemoselective Deprotection with Different Palladium Complexes

    Kamo Naoki, Hayashi Gosuke, Okamoto Akimitsu

    ORGANIC LETTERS   Vol. 21 ( 20 ) page: 8378 - 8382   2019.10

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    DOI: 10.1021/acs.orglett.9b03152

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  17. Cysteinylprolyl imide (CPI) peptide: a highly reactive and easily accessible crypto-thioester for chemical protein synthesis

    Yanase Masafumi, Nakatsu Koki, Cardos Charlane Joy, Konda Yoshiki, Hayashi Gosuke, Okamoto Akimitsu

    CHEMICAL SCIENCE   Vol. 10 ( 23 ) page: 5967 - 5975   2019.6

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    DOI: 10.1039/c9sc00646j

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  18. Reaction design for highly efficient chemical protein synthesis

    Hayashi Gosuke, Okamoto Akimitsu

    ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY   Vol. 257   page: .   2019.3

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  19. Simultaneous and Traceless Ligation of Peptide Fragments on DNA Scaffold.

    Hayashi G, Yanase M, Nakatsuka Y, Okamoto A

    Biomacromolecules   Vol. 20 ( 3 ) page: 1246 - 1253   2019.3

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    DOI: 10.1021/acs.biomac.8b01655

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  20. Triple Function of 4-Mercaptophenylacetic Acid Promotes One-Pot Multiple Peptide Ligation.

    Kamo N, Hayashi G, Okamoto A

    Angewandte Chemie (International ed. in English)   Vol. 57 ( 50 ) page: 16533 - 16537   2018.12

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    DOI: 10.1002/anie.201809765

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  21. Chemistry-Driven Epigenetic Investigation of Histone and DNA Modifications.

    Sueoka T, Koyama K, Hayashi G, Okamoto A

    Chemical record (New York, N.Y.)   Vol. 18 ( 12 ) page: 1727 - 1744   2018.12

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    DOI: 10.1002/tcr.201800040

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  22. Efficient peptide ligation between allyl-protected Asp and Cys followed by palladium-mediated deprotection.

    Kamo N, Hayashi G, Okamoto A

    Chemical communications (Cambridge, England)   Vol. 54 ( 34 ) page: 4337 - 4340   2018.4

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    DOI: 10.1039/c8cc01965g

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  23. Hybridization-sensitive Fluorescent Oligonucleotide Probe Conjugated with Cell-penetrating Peptides for Enhanced Cellular Uptake

    Hayashi Gosuke, Tamai Makoto, Okamoto Akimitsu

    CHEMISTRY LETTERS   Vol. 46 ( 12 ) page: 1803-1806   2017.12

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    DOI: 10.1246/cl.170813

  24. Regulation of the Stability of the Histone H2A-H2B Dimer by H2A Tyr57 Phosphorylation.

    Sueoka T, Hayashi G, Okamoto A

    Biochemistry   Vol. 56 ( 36 ) page: 4767 - 4772   2017.9

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    DOI: 10.1021/acs.biochem.7b00504

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  25. Chemical synthesis of dual labeled proteins via differently protected alkynes enables intramolecular FRET analysis.

    Hayashi G, Kamo N, Okamoto A

    Chemical communications (Cambridge, England)   Vol. 53 ( 43 ) page: 5918 - 5921   2017.5

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    Language:English   Publishing type:Research paper (scientific journal)  

    DOI: 10.1039/c7cc02612a

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  26. Chemically-activatable alkyne-tagged probe for imaging microdomains in lipid bilayer membranes.

    Yamaguchi S, Matsushita T, Izuta S, Katada S, Ura M, Ikeda T, Hayashi G, Suzuki Y, Kobayashi K, Tokunaga K, Ozeki Y, Okamoto A

    Scientific reports   Vol. 7   page: 41007   2017.1

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    Language:English   Publishing type:Research paper (scientific journal)  

    DOI: 10.1038/srep41007

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  27. Base-Resolution Analysis of 5-Hydroxymethylcytosine by One-Pot Bisulfite-Free Chemical Conversion with Peroxotungstate.

    Hayashi G, Koyama K, Shiota H, Kamio A, Umeda T, Nagae G, Aburatani H, Okamoto A

    Journal of the American Chemical Society   Vol. 138 ( 43 ) page: 14178 - 14181   2016.11

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    Publishing type:Research paper (scientific journal)  

    DOI: 10.1021/jacs.6b06428

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  28. In vitro and in cell analysis of chemically synthesized histone H2A with multiple modifications.

    Hayashi G, Sueoka T, Okamoto A

    Chemical communications (Cambridge, England)   Vol. 52 ( 28 ) page: 4999 - 5002   2016.4

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    Publishing type:Research paper (scientific journal)  

    DOI: 10.1039/c5cc10555b

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  29. Diazirine Photocrosslinking Recruits Activated FTO Demethylase Complexes for Specific N-6-methyladenosine Recognition Reviewed

    Hyun Seok Jeong, Gosuke Hayashi, Akimitsu Okamoto

    ACS CHEMICAL BIOLOGY   Vol. 10 ( 6 ) page: 1450 - 5   2015.6

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    Publishing type:Research paper (scientific journal)   Publisher:AMER CHEMICAL SOC  

    N-6-methyladenosine (m(6)A) is a prevalent modification of RNAs. m(6)A exists in mRNA and plays an important role in RNA biological pathways and in RNA epigenetic regulation, We applied diazirine photocrosslinking to the event of m(6)A recognition mediated by the fat mass and obesity associated (FTO) demethylase. A highly photoreactive diazirine adjacent to m(6)A on the RNA successfully recruited activated FTO complexes with an m(6)A preference. The process of recognition of m(6)A via FTO using diazirine photocrosslinking was controlled by the alpha-ketoglutarate (alpha-KG) cosubstrate and the Peal). cofactor, which are involved in m(6)A oxidative demethylation. In addition, FTO bound to ssRNAs prior to the m(6)A recognition process. Diazirine photocrosslinking contributes to increasing the chances of capturing activated FTO complexes with specific m(6)A recognition and provides new insights into the dynamic FTO oxidative demethylation process.

    DOI: 10.1021/cb5010096

    Web of Science

    PubMed

  30. 2-Oxazoline formation for selective chemical labeling of 5-hydroxylysine.

    Hayashi G, Sakamoto R, Okamoto A

    Chemistry, an Asian journal   Vol. 10 ( 5 ) page: 1138 - 41   2015.5

     More details

    Publishing type:Research paper (scientific journal)  

    DOI: 10.1002/asia.201500172

    PubMed

  31. Hybridization-sensitive fluorescent oligonucleotide probe conjugated with a bulky module for compartment-specific mRNA monitoring in a living cell.

    Hayashi G, Yanase M, Takeda K, Sakakibara D, Sakamoto R, Wang DO, Okamoto A

    Bioconjugate chemistry   Vol. 26 ( 3 ) page: 412 - 7   2015.3

     More details

    Publishing type:Research paper (scientific journal)  

    DOI: 10.1021/acs.bioconjchem.5b00090

    PubMed

  32. Middle-Down and Chemical Proteomic Approaches to Reveal Histone H4 Modification Dynamics in Cell Cycle: Label-Free Semi-Quantification of Histone Tail Peptide Modifications Including Phosphorylation and Highly Sensitive Capture of Histone PTM Binding Proteins Using Photo-Reactive Crosslinkers.

    Yamamoto K, Chikaoka Y, Hayashi G, Sakamoto R, Yamamoto R, Sugiyama A, Kodama T, Okamoto A, Kawamura T

    Mass spectrometry (Tokyo, Japan)   Vol. 4 ( 1 ) page: A0039   2015

     More details

    Publishing type:Research paper (scientific journal)  

    DOI: 10.5702/massspectrometry.A0039

    PubMed

  33. An orthogonal ribosome-tRNA pair via engineering of the peptidyl transferase center.

    Terasaka N, Hayashi G, Katoh T, Suga H

    Nature chemical biology   Vol. 10 ( 7 ) page: 555 - 7   2014.7

     More details

    Publishing type:Research paper (scientific journal)  

    DOI: 10.1038/nchembio.1549

    PubMed

  34. Development of photoswitchable RNA aptamer-ligand complexes.

    Hayashi G, Nakatani K

    Methods in molecular biology (Clifton, N.J.)   Vol. 1111   page: 29 - 40   2014

     More details

    Publishing type:Research paper (scientific journal)  

    DOI: 10.1007/978-1-62703-755-6_3

    PubMed

  35. Probe design for the effective fluorescence imaging of intracellular RNA.

    Hayashi G, Okamoto A

    Chemical record (New York, N.Y.)   Vol. 13 ( 2 ) page: 209 - 17   2013.4

     More details

    Publishing type:Research paper (scientific journal)  

    DOI: 10.1002/tcr.201200026

    PubMed

  36. A nucleic acid probe labeled with desmethyl thiazole orange: a new type of hybridization-sensitive fluorescent oligonucleotide for live-cell RNA imaging.

    Okamoto A, Sugizaki K, Yuki M, Yanagisawa H, Ikeda S, Sueoka T, Hayashi G, Wang DO

    Organic & biomolecular chemistry   Vol. 11 ( 2 ) page: 362 - 71   2013.1

     More details

    Publishing type:Research paper (scientific journal)  

    DOI: 10.1039/c2ob26707a

    PubMed

  37. Activation of prokaryotic translation by antisense oligonucleotides binding to coding region of mRNA.

    Hayashi G, Hong C, Hagihara M, Nakatani K

    Biochemical and biophysical research communications   Vol. 429 ( 1-2 ) page: 105 - 10   2012.12

     More details

    Publishing type:Research paper (scientific journal)  

    DOI: 10.1016/j.bbrc.2012.10.072

    PubMed

  38. The RNA origin of transfer RNA aminoacylation and beyond.

    Suga H, Hayashi G, Terasaka N

    Philosophical transactions of the Royal Society of London. Series B, Biological sciences   Vol. 366 ( 1580 ) page: 2959 - 64   2011.10

     More details

    Publishing type:Research paper (scientific journal)  

    DOI: 10.1098/rstb.2011.0137

    PubMed

  39. [Ribosomal synthesis of nonstandard cyclic peptides and its application to drug discovery].

    Hayashi G, Ohshiro Y, Suga H

    Seikagaku. The Journal of Japanese Biochemical Society   Vol. 82 ( 6 ) page: 505-14   2010.6

     More details

    Language:Japanese   Publishing type:Research paper (scientific journal)  

  40. [Ribosomal synthesis of nonstandard cyclic peptides and its application to drug discovery].

    Hayashi G, Ohshiro Y, Suga H

    Seikagaku. The Journal of Japanese Biochemical Society   Vol. 82 ( 6 ) page: 505 - 14   2010.6

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    Publishing type:Research paper (scientific journal)  

    PubMed

  41. Ribosome evolution for two artificial amino acids in E. coli. International journal

    Hayashi G, Goto Y, Suga H

    Chemistry & biology   Vol. 17 ( 4 ) page: 320 - 1   2010.4

     More details

    Language:English   Publishing type:Research paper (scientific journal)  

    DOI: 10.1016/j.chembiol.2010.04.005

    PubMed

  42. RNA aptamers that reversibly bind photoresponsive azobenzene-containing peptides.

    Hayashi G, Hagihara M, Nakatani K

    Chemistry (Weinheim an der Bergstrasse, Germany)   Vol. 15 ( 2 ) page: 424 - 32   2009

     More details

    Publishing type:Research paper (scientific journal)  

    DOI: 10.1002/chem.200800936

    PubMed

  43. Genotyping by allele-specific L-DNA-tagged PCR.

    Hayashi G, Hagihara M, Nakatani K

    Journal of biotechnology   Vol. 135 ( 2 ) page: 157 - 60   2008.6

     More details

    Publishing type:Research paper (scientific journal)  

    DOI: 10.1016/j.jbiotec.2008.03.011

    PubMed

  44. RNA aptamers that reversibly bind to photoresponsive peptide.

    Hayashi G, Hagihara M, Nakatani K

    Nucleic acids symposium series (2004)   ( 52 ) page: 703 - 4   2008

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    Publishing type:Research paper (scientific journal)  

    DOI: 10.1093/nass/nrn355

    PubMed

  45. Photoregulation of a peptide-RNA interaction on a gold surface.

    Hayashi G, Hagihara M, Dohno C, Nakatani K

    Journal of the American Chemical Society   Vol. 129 ( 28 ) page: 8678 - 9   2007.7

     More details

    Publishing type:Research paper (scientific journal)  

    DOI: 10.1021/ja071298x

    PubMed

  46. Detection of L-DNA-tagged PCR products by surface plasmon resonance imaging.

    Hayashi G, Hagihara M, Kobori A, Nakatani K

    Chembiochem : a European journal of chemical biology   Vol. 8 ( 2 ) page: 169 - 71   2007.1

     More details

    Publishing type:Research paper (scientific journal)  

    DOI: 10.1002/cbic.200600477

    PubMed

  47. Reversible regulation of binding between a photoresponsive peptide and its RNA aptamer.

    Hayashi G, Hagihara M, Dohno C, Nakatani K

    Nucleic acids symposium series (2004)   ( 51 ) page: 93 - 4   2007

     More details

    Publishing type:Research paper (scientific journal)  

    DOI: 10.1093/nass/nrm047

    PubMed

  48. N,N'-Bis(3-aminopropyl)-2,7-diamino-1,8-naphthyridine stabilized a single pyrimidine bulge in duplex DNA.

    Suda H, Kobori A, Zhang J, Hayashi G, Nakatani K

    Bioorganic & medicinal chemistry   Vol. 13 ( 14 ) page: 4507 - 12   2005.7

     More details

    Publishing type:Research paper (scientific journal)  

    DOI: 10.1016/j.bmc.2005.04.035

    PubMed

  49. Small-molecule ligand induces nucleotide flipping in (CAG)n trinucleotide repeats.

    Nakatani K, Hagihara S, Goto Y, Kobori A, Hagihara M, Hayashi G, Kyo M, Nomura M, Mishima M, Kojima C

    Nature chemical biology   Vol. 1 ( 1 ) page: 39 - 43   2005.6

     More details

    Publishing type:Research paper (scientific journal)  

    DOI: 10.1038/nchembio708

    PubMed

  50. Application of L-DNA as a molecular tag.

    Hayashi G, Hagihara M, Nakatani K

    Nucleic acids symposium series (2004)   ( 49 ) page: 261 - 2   2005

     More details

    Publishing type:Research paper (scientific journal)  

    DOI: 10.1093/nass/49.1.261

    PubMed

  51. Solution structure of a small-molecular ligand complexed with CAG trinucleotide repeat DNA.

    Nakatani K, Hagihara S, Goto Y, Kobori A, Hagihara M, Hayashi G, Kyo M, Nomura M, Mishima M, Kojima C

    Nucleic acids symposium series (2004)   ( 49 ) page: 49 - 50   2005

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    Publishing type:Research paper (scientific journal)  

    DOI: 10.1093/nass/49.1.49

    PubMed

  52. Detection of guanine-adenine mismatches by surface plasmon resonance sensor carrying naphthyridine-azaquinolone hybrid on the surface. International journal

    Hagihara S, Kumasawa H, Goto Y, Hayashi G, Kobori A, Saito I, Nakatani K

    Nucleic acids research   Vol. 32 ( 1 ) page: 278 - 86   2004

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    Language:English   Publishing type:Research paper (scientific journal)  

    We have discovered a new molecule naphthyridine-azaquinolone hybrid (Npt-Azq) that strongly stabilized the guanine-adenine (G-A) mismatch in duplex DNA. In the presence of Npt-Azq, the melting temperature (T(m)) of 5'-d(CTA ACG GAA TG)-3'/3'-d(GAT TGA CTT AC)-5' containing a single G-A mismatch increased by 15.4 degrees C, whereas fully matched duplex increased its T(m) only by 2.2 degrees C. Npt-Azq was immobilized on the sensor surface for the surface plasmon resonance (SPR) assay to examine SPR detection of duplexes containing a G-A mismatch. Distinct SPR signals were observed when 27mer DNA containing a G-A mismatch was analyzed by the Npt-Azq immobilized sensor surfaces, whereas the signal of the fully matched duplex was approximately 6-fold weaker in intensity. The SPR signals for the G-A mismatch were proportional to the concentration of DNA in a range up to 1 microM, confirming that the SPR signal is in fact due to the binding of the G-A mismatch to Npt-Azq immobilized on the surface. Examination of all 16 G-A mismatches regarding the flanking sequence revealed that the sensor surface reported here is applicable to eight flanking sequences, covering 50% of all possible G-A mismatches.

    DOI: 10.1093/nar/gkh171

    PubMed

  53. SPR fingerprinting of mismatched base pair.

    Kobori A, Peng T, Hayashi G, Nakatani K

    Nucleic acids symposium series (2004)   ( 48 ) page: 129 - 30   2004

     More details

    Publishing type:Research paper (scientific journal)  

    DOI: 10.1093/nass/48.1.129

    PubMed

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MISC 28

  1. Reaction design for highly efficient chemical protein synthesis

    Hayashi Gosuke, Okamoto Akimitsu

    ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY   Vol. 257   page: .   2019.3

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    Language:English  

    Web of Science

  2. Hybridization-sensitive Fluorescent Oligonucleotide Probe Conjugated with Cell-penetrating Peptides for Enhanced Cellular Uptake

    Hayashi Gosuke, Tamai Makoto, Okamoto Akimitsu

    CHEMISTRY LETTERS   Vol. 46 ( 12 ) page: 1803-1806   2017.12

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    Language:English  

    DOI: 10.1246/cl.170813

    Web of Science

  3. Base-Resolution Analysis of 5-Hydroxymethylcytosine by One-Pot Bisulfite-Free Chemical Conversion with Peroxotungstate.

    Hayashi G, Koyama K, Shiota H, Kamio A, Umeda T, Nagae G, Aburatani H, Okamoto A

    Journal of the American Chemical Society   Vol. 138 ( 43 ) page: 14178-14181   2016.11

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    Language:English  

    DOI: 10.1021/jacs.6b06428

    PubMed

  4. In vitro and in cell analysis of chemically synthesized histone H2A with multiple modifications.

    Hayashi G, Sueoka T, Okamoto A

    Chemical communications (Cambridge, England)   Vol. 52 ( 28 ) page: 4999-5002   2016.4

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    Language:English  

    DOI: 10.1039/c5cc10555b

    PubMed

  5. Diazirine photocrosslinking recruits activated FTO demethylase complexes for specific N(6)-methyladenosine recognition.

    Jeong HS, Hayashi G, Okamoto A

    ACS chemical biology   Vol. 10 ( 6 ) page: 1450-5   2015.6

     More details

    Language:English  

    DOI: 10.1021/cb5010096

    PubMed

  6. 2-Oxazoline formation for selective chemical labeling of 5-hydroxylysine.

    Hayashi G, Sakamoto R, Okamoto A

    Chemistry, an Asian journal   Vol. 10 ( 5 ) page: 1138-41   2015.5

     More details

    Language:English  

    DOI: 10.1002/asia.201500172

    PubMed

  7. Hybridization-sensitive fluorescent oligonucleotide probe conjugated with a bulky module for compartment-specific mRNA monitoring in a living cell.

    Hayashi G, Yanase M, Takeda K, Sakakibara D, Sakamoto R, Wang DO, Okamoto A

    Bioconjugate chemistry   Vol. 26 ( 3 ) page: 412-7   2015.3

     More details

    Language:English  

    DOI: 10.1021/acs.bioconjchem.5b00090

    PubMed

  8. Middle-Down and Chemical Proteomic Approaches to Reveal Histone H4 Modification Dynamics in Cell Cycle: Label-Free Semi-Quantification of Histone Tail Peptide Modifications Including Phosphorylation and Highly Sensitive Capture of Histone PTM Binding Proteins Using Photo-Reactive Crosslinkers.

    Yamamoto K, Chikaoka Y, Hayashi G, Sakamoto R, Yamamoto R, Sugiyama A, Kodama T, Okamoto A, Kawamura T

    Mass spectrometry (Tokyo, Japan)   Vol. 4 ( 1 ) page: A0039   2015

     More details

    Language:English  

    DOI: 10.5702/massspectrometry.A0039

    PubMed

  9. An orthogonal ribosome-tRNA pair via engineering of the peptidyl transferase center.

    Terasaka N, Hayashi G, Katoh T, Suga H

    Nature chemical biology   Vol. 10 ( 7 ) page: 555-7   2014.7

     More details

    Language:English  

    DOI: 10.1038/nchembio.1549

    PubMed

  10. Development of photoswitchable RNA aptamer-ligand complexes.

    Hayashi G, Nakatani K

    Methods in molecular biology (Clifton, N.J.)   Vol. 1111   page: 29-40   2014

     More details

    Language:English  

    DOI: 10.1007/978-1-62703-755-6_3

    PubMed

  11. Probe design for the effective fluorescence imaging of intracellular RNA.

    Hayashi G, Okamoto A

    Chemical record (New York, N.Y.)   Vol. 13 ( 2 ) page: 209-17   2013.4

     More details

    Language:English  

    DOI: 10.1002/tcr.201200026

    PubMed

  12. A nucleic acid probe labeled with desmethyl thiazole orange: a new type of hybridization-sensitive fluorescent oligonucleotide for live-cell RNA imaging.

    Okamoto A, Sugizaki K, Yuki M, Yanagisawa H, Ikeda S, Sueoka T, Hayashi G, Wang DO

    Organic & biomolecular chemistry   Vol. 11 ( 2 ) page: 362-71   2013.1

     More details

    Language:English  

    DOI: 10.1039/c2ob26707a

    PubMed

  13. Activation of prokaryotic translation by antisense oligonucleotides binding to coding region of mRNA.

    Hayashi G, Hong C, Hagihara M, Nakatani K

    Biochemical and biophysical research communications   Vol. 429 ( 1-2 ) page: 105-10   2012.12

     More details

    Language:English  

    DOI: 10.1016/j.bbrc.2012.10.072

    PubMed

  14. The RNA origin of transfer RNA aminoacylation and beyond.

    Suga H, Hayashi G, Terasaka N

    Philosophical transactions of the Royal Society of London. Series B, Biological sciences   Vol. 366 ( 1580 ) page: 2959-64   2011.10

     More details

    Language:English  

    DOI: 10.1098/rstb.2011.0137

    PubMed

  15. [Ribosomal synthesis of nonstandard cyclic peptides and its application to drug discovery].

    Hayashi G, Ohshiro Y, Suga H

    Seikagaku. The Journal of Japanese Biochemical Society   Vol. 82 ( 6 ) page: 505-14   2010.6

     More details

    Language:Japanese  

    PubMed

  16. Ribosome evolution for two artificial amino acids in E. coli.

    Hayashi G, Goto Y, Suga H

    Chemistry & biology   Vol. 17 ( 4 ) page: 320-1   2010.4

     More details

    Language:English  

    DOI: 10.1016/j.chembiol.2010.04.005

    PubMed

  17. RNA aptamers that reversibly bind photoresponsive azobenzene-containing peptides.

    Hayashi G, Hagihara M, Nakatani K

    Chemistry (Weinheim an der Bergstrasse, Germany)   Vol. 15 ( 2 ) page: 424-32   2009

     More details

    Language:English  

    DOI: 10.1002/chem.200800936

    PubMed

  18. Genotyping by allele-specific L-DNA-tagged PCR.

    Hayashi G, Hagihara M, Nakatani K

    Journal of biotechnology   Vol. 135 ( 2 ) page: 157-60   2008.6

     More details

    Language:English  

    DOI: 10.1016/j.jbiotec.2008.03.011

    PubMed

  19. RNA aptamers that reversibly bind to photoresponsive peptide.

    Hayashi G, Hagihara M, Nakatani K

    Nucleic acids symposium series (2004)   ( 52 ) page: 703-4   2008

     More details

    Language:English  

    DOI: 10.1093/nass/nrn355

    PubMed

  20. Photoregulation of a peptide-RNA interaction on a gold surface.

    Hayashi G, Hagihara M, Dohno C, Nakatani K

    Journal of the American Chemical Society   Vol. 129 ( 28 ) page: 8678-9   2007.7

     More details

    Language:English  

    DOI: 10.1021/ja071298x

    PubMed

  21. Detection of L-DNA-tagged PCR products by surface plasmon resonance imaging.

    Hayashi G, Hagihara M, Kobori A, Nakatani K

    Chembiochem : a European journal of chemical biology   Vol. 8 ( 2 ) page: 169-71   2007.1

     More details

    Language:English  

    DOI: 10.1002/cbic.200600477

    PubMed

  22. Reversible regulation of binding between a photoresponsive peptide and its RNA aptamer.

    Hayashi G, Hagihara M, Dohno C, Nakatani K

    Nucleic acids symposium series (2004)   ( 51 ) page: 93-4   2007

     More details

    Language:English  

    DOI: 10.1093/nass/nrm047

    PubMed

  23. N,N'-Bis(3-aminopropyl)-2,7-diamino-1,8-naphthyridine stabilized a single pyrimidine bulge in duplex DNA.

    Suda H, Kobori A, Zhang J, Hayashi G, Nakatani K

    Bioorganic & medicinal chemistry   Vol. 13 ( 14 ) page: 4507-12   2005.7

     More details

    Language:English  

    DOI: 10.1016/j.bmc.2005.04.035

    PubMed

  24. Small-molecule ligand induces nucleotide flipping in (CAG)n trinucleotide repeats.

    Nakatani K, Hagihara S, Goto Y, Kobori A, Hagihara M, Hayashi G, Kyo M, Nomura M, Mishima M, Kojima C

    Nature chemical biology   Vol. 1 ( 1 ) page: 39-43   2005.6

     More details

    Language:English  

    DOI: 10.1038/nchembio708

    PubMed

  25. Application of L-DNA as a molecular tag.

    Hayashi G, Hagihara M, Nakatani K

    Nucleic acids symposium series (2004)   ( 49 ) page: 261-2   2005

     More details

    Language:English  

    DOI: 10.1093/nass/49.1.261

    PubMed

  26. Solution structure of a small-molecular ligand complexed with CAG trinucleotide repeat DNA.

    Nakatani K, Hagihara S, Goto Y, Kobori A, Hagihara M, Hayashi G, Kyo M, Nomura M, Mishima M, Kojima C

    Nucleic acids symposium series (2004)   ( 49 ) page: 49-50   2005

     More details

    Language:English  

    DOI: 10.1093/nass/49.1.49

    PubMed

  27. SPR fingerprinting of mismatched base pair.

    Kobori A, Peng T, Hayashi G, Nakatani K

    Nucleic acids symposium series (2004)   ( 48 ) page: 129-30   2004

     More details

    Language:English  

    DOI: 10.1093/nass/48.1.129

    PubMed

  28. Detection of guanine-adenine mismatches by surface plasmon resonance sensor carrying naphthyridine-azaquinolone hybrid on the surface.

    Hagihara S, Kumasawa H, Goto Y, Hayashi G, Kobori A, Saito I, Nakatani K

    Nucleic acids research   Vol. 32 ( 1 ) page: 278-86   2004

     More details

    Language:English  

    DOI: 10.1093/nar/gkh171

    PubMed

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Research Project for Joint Research, Competitive Funding, etc. 2

  1. Sタンパク質結合人工抗体を用いたコロナウィルス濃縮および抗原検査法の開発

    2020.7 - 2021.6

    出資金による受託研究 

  2. 有機化学を基盤としたエピゲノム修飾ヌク レオソーム再構成技術の確立

    2019.10 - 2023.3

    特色ある大学教育支援プログラム 

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    Grant type:Competitive

KAKENHI (Grants-in-Aid for Scientific Research) 16

  1. タンパク質化学合成と進化分子工学を活用したユビキチンケモテクノロジーの創出

    Grant number:21H00278  2021.4 - 2023.3

    科学研究費助成事業  新学術領域研究(研究領域提案型)

    林 剛介

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    Authorship:Principal investigator 

    Grant amount:\7280000 ( Direct Cost: \5600000 、 Indirect Cost:\1680000 )

    本研究では、タンパク質化学合成の方法を用いてユビキチン化タンパク質を作製するが、その標的として、A)翻訳の品質管理機構に関わるリボソームタンパク質、B)維持メチル化機構に関わるPAF15、C)ヘテロクロマチン形成に関わるHP1αおよびヒストンH2A、などを選択する。化学合成で作製されたユビキチン化タンパク質やその他のユビキチン関連タンパク質(例えばプロテアソームのサブユニットであるRPN10など)に結合する人工抗体は、申請者の研究グループで開発されたin vitroセレクション法である「TRAPディスプレイ法」を用いて取得する。

  2. Sタンパク質結合人工抗体を用いたコロナウィルス濃縮および抗原検査法の開発

    2020.7 - 2021.6

    出資金による受託研究 

      More details

    Grant type:Competitive

  3. 生体分子夾雑系で機能するD体人工抗体の開発

    2020.4 - 2022.3

    科学研究費補助金 

      More details

    Authorship:Principal investigator 

  4. 生体分子夾雑系で機能するD体人工抗体の開発

    2020.4 - 2022.3

    科学研究費助成事業  新学術領域研究(研究領域提案型)

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    Grant type:Competitive

  5. Mirror-image Artificial Antibody Working in Multimolecular Crowding Biosystems

    Grant number:20H04704  2020.4 - 2022.3

    Grants-in-Aid for Scientific Research  Grant-in-Aid for Scientific Research on Innovative Areas (Research in a proposed research area)

      More details

    Authorship:Principal investigator 

    Grant amount:\4940000 ( Direct Cost: \3800000 、 Indirect Cost:\1140000 )

  6. 有機化学を基盤としたエピゲノム修飾ヌク レオソーム再構成技術の確立

    2019.10 - 2023.3

    文部科学省  戦略的創造研究推進事業 

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    Grant type:Competitive

  7. Efficient Chemical Synthesis of Polyubiquitin and Ubiquitinated Proteins

    Grant number:19H05287  2019.4 - 2021.3

    Grant-in-Aid for Scientific Research on Innovative Areas (Research in a proposed research area)

      More details

    Authorship:Principal investigator 

    Grant amount:\5070000 ( Direct Cost: \3900000 、 Indirect Cost:\1170000 )

  8. DNAを足場としたペプチド断片の同時連結反応によるタンパク質の効率的化学合成

    2018.4 - 2021.3

    科学研究費補助金  基盤研究(C)

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    Authorship:Principal investigator 

  9. DNAを足場としたペプチド断片の同時連結反応によるタンパク質の効率的化学合成

    2018.4 - 2021.3

    日本学術振興会  科学研究費助成事業  基盤研究(C)

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    Grant type:Competitive

  10. Chemical synthesis of protein via simultaneous ligation of multiple peptide segments on DNA scaffold

    Grant number:18K05313  2018.4 - 2021.3

    Grants-in-Aid for Scientific Research  Grant-in-Aid for Scientific Research (C)

    Hayashi Gosuke

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    Authorship:Principal investigator 

    Grant amount:\4420000 ( Direct Cost: \3400000 、 Indirect Cost:\1020000 )

    We have developed a novel peptide ligation strategy harnessing the two intrinsic characteristics of oligodeoxynucleotides (ODNs), i.e., their hydrophilicity and hybridization ability, which allowed an increase in the water solubility of peptides and the reaction kinetics due to the proximity effect, respectively. Peptide&#8211;ODN conjugates cleavable to regenerate native peptide sequences were synthesized using novel lysine derivatives containing conjugation handles and photolabile linkers, via solid-phase peptide synthesis and subsequent conjugation to 15-mer ODNs. Two complementary conjugates were applied to carbodiimide-mediated peptide ligation on a DNA scaffold and the subsequent DNA removal was conducted by photoirradiation in a traceless fashion.

  11. 分解反応の遷移状態構造に立脚した新型核酸医薬を志向した核酸酵素の創製

    2015.7 - 2018.3

    科学研究費補助金  基盤研究(B)

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    Authorship:Coinvestigator(s) 

  12. 分解反応の遷移状態構造に立脚した新型核酸医薬を志向した核酸酵素の創製

    2015.7 - 2018.3

    日本学術振興会  科学研究費助成事業  基盤研究(B)

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    Grant type:Competitive

  13. Development of nucleic acid enzymes for new nucleic acid medicines based on the transition state in molecular degradation

    Grant number:15KT0057  2015.7 - 2018.3

    Okamoto Akimitsu

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    Authorship:Coinvestigator(s) 

    The solid-state fermentation (SSF) bioprocesses are performed in complex solid-rich systems that present significant challenges for effective monitoring of bacterial population dynamics. We have developed an efficient chemical system that allows quantification of bacteria population by fluorescence-based analysis. The key component in the system is the exciton-controlled fluorescent RNA aptamer, which was covalently conjugated to two thiazole orange moieties and serves as a competitor of bacterial ribosome. The intensity of fluorescence from such a ribosome-sensing system was controlled by the excitonic interaction between dyes in the RNA aptamer and it increased drastically in the presence of Escherichia coli. This innovative fluorescence-based competition system is valuable for quantification without any extraction of bacterial nucleic acids, and provides the simplest and most feasible way to optimize SSF bioprocesses.

  14. ヒストンコード研究の基盤となる多様な修飾を有するヌクレオソーム構築法の開発と応用

    2013.4 - 2015.3

    科学研究費補助金  若手研究(B)

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    Authorship:Principal investigator 

  15. ヒストンコード研究の基盤となる多様な修飾を有するヌクレオソーム構築法の開発と応用

    2013.4 - 2015.3

    日本学術振興会  科学研究費助成事業  若手研究(B)

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    Grant type:Competitive

  16. Development of a platform for histone-code research by setting nucleosomes with various modifications

    Grant number:25870186  2013.4 - 2015.3

    HAYASHI Gosuke

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    Authorship:Principal investigator 

    Grant amount:\4290000 ( Direct Cost: \3300000 、 Indirect Cost:\990000 )

    We developed a chemical platform for approaching “histone code hypothesis”, that is one of the most important issues in epigenetics research. Total chemical synthesis of core histone H2A, H2B, and linker histone H1, all of which play essential roles in gene regulation and chromatin integrity, have been achieved by solid-phase peptide synthesis (SPPS) and native chemical ligation (NCL). The chemically-synthesized histones showed comparable ability to form nucleosome and chromatosome in vitro. Furthermore, we introduced dye-labelled H2A into HeLa cells and observed that the synthetic histone protein successfully localized into nucleus.

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Teaching Experience (On-campus) 12

  1. 分析化学2

    2020

  2. 生体分子応用化学

    2020

  3. 分析化学3

    2020

  4. 化学生命工学実験3

    2020

  5. 分子生命化学基礎論

    2020

  6. 化学実験

    2020

  7. 化学生命工学実験1

    2020

  8. 分析化学3

    2019

  9. 化学生命工学実験1

    2019

  10. 分析化学2

    2019

  11. 化学生命工学実験3

    2019

  12. G30 Core-Biochemistry

    2019

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Teaching Experience (Off-campus) 13

  1. G30 Core-Biochemistry

    Nagoya University)

  2. 生体分子応用化学

    Nagoya University)

  3. 化学生命工学実験3

    Nagoya University)

  4. 化学生命工学実験3

    Nagoya University)

  5. 化学生命工学実験1

    Nagoya University)

  6. 化学生命工学実験1

    Nagoya University)

  7. 化学実験

    Nagoya University)

  8. 分析化学3

    Nagoya University)

  9. 分析化学3

    Nagoya University)

  10. 分析化学2

    Nagoya University)

  11. 分析化学2

    Nagoya University)

  12. 分子生命化学基礎論

    Nagoya University)

  13. G30 Core-Biochemistry

    Nagoya University)

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