Updated on 2024/09/30

写真a

 
SUYAMA KEITARO
 
Organization
Faculty of Arts and Science Division for Experimental Natural Science Assistant Professor
Title
Assistant Professor
Contact information
メールアドレス
Tel
0928025849
Profile
核内受容体に結合する内分泌撹乱物質の探索研究、ならびに核内受容体結合試験のための新規分子ツールの創製の研究を行っている。また、核内受容体に結合し生理活性を示す化合物の分子設計・合成も行っている。 これらの研究目的を達成するため、ペプチドおよび小分子の有機化合物の合成、分光分析、物理化学的解析および計算化学による分析を実施している。
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Research Areas

  • Nanotechnology/Materials / Bio chemistry

Degree

  • Doctor of Science

Research History

  • Kyushu University Assistant Professor

    2013.4 - Present

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Research Interests・Research Keywords

  • Research theme:peptide science

    Keyword:peptide science

    Research period: 2024

  • Research theme:nuclear receptor

    Keyword:nuclear receptor

    Research period: 2024

  • Research theme:biochemistry

    Keyword:biochemistry

    Research period: 2024

  • Research theme:Coacervation Property and Secondary Structure of the Elastin-derived Synthetic Dimer Peptides

    Keyword:elastin peptide coacervation

    Research period: 2013.3 - 2017.3

  • Research theme:Probe exploitation for essential nuclear receptor-binding assay

    Keyword:nuclear receptor, receptor binding assay, fluorescent probe, bisphenol

    Research period: 2009.4

  • Research theme:Asymmetric reaction caltalyzed by aluminum(salalen) complex

    Keyword:asymmetric catalytic reaction, aluminum(salalen) complex

    Research period: 2006.4 - 2009.3

Awards

  • 日本ペプチド学会 奨励賞

    2023.11   日本ペプチド学会   エラスチン様ペプチド・(FPGVG)n アナログの温度応答性自己集合能に関与する分子機構の解明ならびに分子素材への応用

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    Elastin-like peptides (ELPs) are well-known biopolymers that exhibit temperature-dependent reversible self-assembly. Our research group demonstrated that an ELP consisting of repeated (FPGVG) sequences exhibited a strong self-assembly ability, even with a short peptide chain length. Based on this sequence, short ELP analogs with improved self-assembly abilities were developed. Studies on the structural changes involved in the self-assembly have demonstrated the importance of the (FPGV) sequence for reversible self-assembly. In addition, these short ELP analogs are useful thermoresponsive biomolecular materials.

  • JPS Award for Young Investigator

    2023.11   The Japanese Peptide Society   Investigation of the molecular mechanism involved in the temperature-responsive self-assembly of elastin-like peptide (FPGVG)n analogs and their application in molecular materials

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  • 令和3年度 日本生化学会九州支部 学術奨励賞

    2021.6   日本生化学会九州支部   エラスチンのアミノ酸配列を母体とした温度応答性ペプチド・(FPGVG)nアナログの自己集合能と分子構造に関する研究

  • 優秀ポスター発表賞

    2011.9   泉屋コロキウム   巣山慶太郎:リガンド結合ポケットに遊離システインを含む核内受容体RXRに結合する化学物質の探索. 第11回泉屋コロキウム、国民宿舎 めかり山荘、2011年9月7-8日 (演題番号9).

Papers

  • Enhancement of Aggregate Formation Through Aromatic Compound Adsorption in Elastin-like Peptide (FPGVG)5 Analogs. International journal

    Keitaro Suyama, Masayuki Murashima, Iori Maeda, Takeru Nose

    Biomacromolecules   24 ( 11 )   5265 - 5276   2023.11   ISSN:1525-7797 eISSN:1526-4602

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

    Elastin-like peptides (ELPs) exhibit temperature-dependent reversible self-assembly. Repetitive sequences derived from elastin, such as Val-Pro-Gly-Val-Gly (VPGVG), are essential for the self-assembly of ELPs. Previously, we developed (FPGVG)5 (F5), in which the first valine residue in the VPGVG sequence was replaced with phenylalanine, which showed strong self-aggregation ability. This suggests that interactions through the aromatic amino acid residues of ELPs could play an important role in self-assembly. In this study, we investigated the thermoresponsive behavior of F5 analogs in the presence of aromatic compounds. Turbidimetry, spectroscopy, and fluorescence measurements demonstrated that aromatic compounds interacted with F5 analogs below the transition temperature and enhanced the self-assembly ability of ELPs by stabilizing amyloid-like structures. Furthermore, quantitative high-performance liquid chromatography analyses showed that the F5 analogs could adsorb and remove hydrophobic aromatic compounds from aqueous solutions during aggregate formation. These results suggested that the F5 analogs can be applicable as scavengers of aromatic compounds.

    DOI: 10.1021/acs.biomac.3c00779

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  • Determining the sequence-dependency of self-assembly of elastin-like peptides using short peptide analogs with shuffled repetitive sequences Invited Reviewed International journal

    Daiki Tatsubo, Keitaro Suyama, Naoki Sakamoto, Keisuke Tomohara, Suguru Taniguchi, Iori Maeda, Takeru Nose

    Biochemistry   62 ( 17 )   2559 - 2570   2023.8

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

    DOI: https://doi.org/10.1021/acs.biochem.3c00146

  • Development of the efficient preparation method for thermoresponsive elastin‐like peptides using liquid‐phase synthesis combined with fragment condensation strategy Reviewed

    Kohei Yoshida, Keitaro Suyama, Shin Matsushita, Iori Maeda, Takeru Nose

    Journal of Peptide Science   29 ( 12 )   e3528   2023.6   ISSN:1075-2617 eISSN:1099-1387

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

    DOI: 10.1002/psc.3528

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  • Development of truncated elastin-like peptide analogues with improved temperature-response and self-assembling properties

    Shogo Sumiyoshi, Keitaro Suyama, Naoki Tanaka, Takumi Andoh, Akihiko Nagata, Keisuke Tomohara, Suguru Taniguchi, Iori Maeda, Takeru Nose

    Scientific Reports   12 ( 1 )   19414   2022.11   ISSN:2045-2322 eISSN:2045-2322

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    Language:English   Publishing type:Research paper (scientific journal)   Publisher:Springer Science and Business Media LLC  

    Abstract

    Functional peptides, which are composed of proteinogenic natural amino acids, are expected to be used as biomaterials with minimal environmental impact. Synthesizing a functional peptide with a shorter amino acid sequence while retaining its function is a easy and economical strategy. Furthermore, shortening functional peptides helps to elucidate the mechanism of their functional core region. Truncated elastin-like peptides (ELPs) are peptides consisting of repetitive sequences, derived from the elastic protein tropoelastin, that show the thermosensitive formation of coacervates. In this study, to obtain shortened ELP analogues, we synthesized several (Phe-Pro-Gly-Val-Gly)<sub>n</sub> (FPGVG)<sub>n</sub> analogues with one or two amino acid residues deleted from each repeat sequence, such as the peptide analogues consisting of FPGV and/or FPG sequences. Among the novel truncated ELP analogues, the 16-mer (FPGV)<sub>4</sub> exhibited a stronger coacervation ability than the 25-mer (FPGVG)<sub>5</sub>. These results indicated that the coacervation ability of truncated ELPs was affected by the amino acid sequence and not by the peptide chain length. Based on this finding, we prepared Cd<sup>2+</sup>-binding sequence-conjugated ELP analogue, AADAAC-(FPGV)<sub>4</sub>, and found that it could capture Cd<sup>2+</sup>. These results indicated that the 16-mer (FPGV)<sub>4</sub> only composed of proteinogenic amino acids could be a new biomaterial with low environmental impact.

    DOI: 10.1038/s41598-022-23940-0

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    Other Link: https://www.nature.com/articles/s41598-022-23940-0

  • Flexible customization of the self-assembling abilities of short elastin-like peptide Fn analogs by substituting N-terminal amino acids

    Keitaro Suyama, Marin Shimizu, Iori Maeda, Takeru Nose

    BIOPOLYMERS   113 ( 10 )   e23521   2022.7   ISSN:0006-3525 eISSN:1097-0282

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

    Elastin-like peptides (ELPs) are thermoresponsive biopolymers inspired by the characteristic repetitive sequences of natural elastin. As ELPs exhibit temperature-dependent reversible self-assembly, they are expected to be biocompatible thermoresponsive materials for drug delivery carriers. One of the most widely studied ELPs in this field is the repetitive pentapeptide, (VPGXG)(n). We previously reported that phenylalanine-containing ELP (Fn) analogs, in which the former Val residue of the repetitive sequence (VPGVG)(n) is replaced by Phe, show coacervation with a short chain length (n = 5). Owing to their short sequences, Fn analogs are easily modified in amino acid sequences via simple chemical synthesis, and are useful for investigating the relationship between peptide sequences and temperature responsiveness. In this study, we developed Fn analogs by replacing Phe residue(s) with other amino acids or introducing another amino acid at the N-terminus. The temperature responsiveness of the Fn analogs changed drastically with the substitution of a single Phe residue, suggesting that aromatic amino acids play an important role in their self-assembly. In addition, the self-assembling ability of Fn was enhanced by increasing the bulkiness of the N-terminal amino acids. Therefore, the N-terminal residue was considered to be important for hydrophobicity-induced intermolecular interactions between the peptides during coacervation.

    DOI: 10.1002/bip.23521

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Presentations

  • Regulation of self-assembly ability of short-chain elastin-like peptide (FPGVG)n-azobenzene conjugates by light irradiation

    Keitaro Suyama, Iori Maeda, Takeru Nose

    2024.3 

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    Event date: 2024.3

    Language:English  

    Country:Japan  

  • Investigation of the molecular mechanism involved in the temperature-responsive self-assembly of elastin-like peptide (FPGVG)n analogs and their application in molecular materials Invited

    Keitaro Suyama

    2023.11 

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    Event date: 2023.11 - 2022.11

    Language:English  

    Country:Japan  

  • Light-induced modification of self-assembly in azobenzene-conjugated short elastin-like peptides

    Keitaro Suyama, Iori Maeda, Takeru Nose.

    2023.11 

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    Event date: 2023.11 - 2022.11

    Language:English  

    Country:Japan  

  • 温度応答性エラスチン様ペプチド・(FPGVG) 5アナログの環境中に存在する芳香族化合物への結合特性

    巣山慶太郎、村島幹征、前田衣織、野瀬 健

    第96回日本生化学会大会  2023.11 

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    Event date: 2023.10 - 2024.11

    Language:Japanese  

    Venue:福岡国際会議場   Country:Japan  

  • 短鎖エラスチン様ペプチド・(FPGVG)5の可逆的自己凝集に対する芳香族化合物の影響

    巣山慶太郎、村島幹征、前田衣織、野瀬 健

    令和5年度日本生化学会九州支部例会  2023.6 

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    Event date: 2023.6

    Language:Japanese  

    Venue:長崎大学文教キャンパス   Country:Japan  

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MISC

  • 分野横断的新実験科目「実験を通して学ぶアミノ酸の科学」の開発

    巣山 慶太郎, 野瀬 健

    2017.5

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    Language:Japanese   Publishing type:Internal/External technical report, pre-print, etc.  

    九州大学では平成26年度より、初年時のみならず高年次、大学院教育を通して、自ら学び続けるアクティブ・ラーナー1, 2の育成を目標として掲げた基幹教育を開始した。アクティブ・ラーナーの育成のためには、「専門領域に閉じることなく、分野の垣根を越えて多様な視点から物事を理解し、真理を探求していく態度」を涵養する機会となる科目の開発が必要とされている。そこで、従来の科目の垣根を越えて考える力を持つアクティブ・ラーナーの育成を目指して、著者は新しい実験科目の開発に着手し、試行的に平成27年度後期に総合科目として「実験を通して学ぶアミノ酸の科学」を開講した。本稿では、本科目で実施した授業内容について報告し、また、授業アンケートの結果を交えて、総合科目における実験講義についての受講生の意識について報告した。

Industrial property rights

Patent   Number of applications: 1   Number of registrations: 1
Utility model   Number of applications: 0   Number of registrations: 0
Design   Number of applications: 0   Number of registrations: 0
Trademark   Number of applications: 0   Number of registrations: 0

Professional Memberships

  • 日本化学会

  • 日本ケミカルバイオロジー学会

  • 日本内分泌撹乱化学物質学会

  • 日本ペプチド学会

  • 日本生化学会

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Academic Activities

  • 座長

    日本化学会第104春季年会  ( 日本大学理工学部 船橋キャンパス ) 2024.3 - 2023.3

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    Type:Competition, symposium, etc. 

  • 座長(Chairmanship)

    令和3年度日本生化学会九州支部例会  ( オンライン開催 ) 2021.6

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    Type:Competition, symposium, etc. 

  • ペプチドニュースレター

    2021.1 - 2024.3

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    Type:Academic society, research group, etc. 

  • ペプチドニュースレター

    Role(s): Review, evaluation

    2021.1

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    Type:Peer review 

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  • Screening of academic papers

    Role(s): Peer review

    2021

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    Type:Peer review 

    Number of peer-reviewed articles in foreign language journals:2

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Research Projects

  • 環境水中の有害化学物質除去に資する環境調和型温度応答性ペプチド素材の設計と応用

    Grant number:24K03120  2024.4 - 2028.3

    科学研究費助成事業  基盤研究(B)

    野瀬 健, 友原 啓介, 前田 衣織, 巣山 慶太郎

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    Grant type:Scientific research funding

    本研究では、天然アミノ酸からなる合成ペプチド・短鎖Elastin-like polypeptides(sELP)の温度依存的可逆自己凝集能をもとに、水系から化学物質を吸着・捕集し、相分離により除去する新しい環境適応型短鎖ペプチド性分子素材を開発する。本研究では、1)sELPの温度応答性や凝集特性のアミノ酸配列依存性を解明し、凝集温度の制御を可能とする。2)安価で簡便なsELP調製方法を開発し、sELPの応用可能性を拡大する。これらにより、環境水中の化学物質の吸着(結合)、捕集機能を備えたsELPの開発を目指す。

    CiNii Research

  • ペプチド医薬の超長期滞留性DDSの開発

    2022.9 - 2024.3

    共同研究

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    Authorship:Coinvestigator(s)  Grant type:Other funds from industry-academia collaboration

  • 【AMED橋渡し研究プログラム】九州大学拠点2022年度 異分野融合型研究シーズ(シーズH)

    2022.9 - 2024.3

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    Authorship:Coinvestigator(s) 

  • Development of peptide drug delivery carrier for photodynamic therapy that can control drug release by light irradiation

    Grant number:22K12819  2022 - 2024

    Japan Society for the Promotion of Science  Grants-in-Aid for Scientific Research  Grant-in-Aid for Scientific Research (C)

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    Authorship:Principal investigator  Grant type:Scientific research funding

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  • 天然タンパク質資源の有効活用を目指した機能性マイクロ粒子捕集素材の開発

    Grant number:20K20638  2020.7 - 2024.3

    科学研究費助成事業  挑戦的研究(開拓)

    野瀬 健, 前田 衣織, 友原 啓介, 巣山 慶太郎

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    Grant type:Scientific research funding

    マイクロプラスチックの環境汚染が問題となる中、それらを捕集するための素材を、現在利用が進んでいない天然由来タンパク質を母体として調製することを目的とする。特に、タンパク質を高機能化するために感温性ペプチドで架橋することにより温度に依存して変化する網目構造を構築することを試みる。温度依存的に構造変化するタンパク質・エラスチンをモデルとして、エラスチン様ペプチドによる架橋反応をタンパク質に施しプラスチック粒子のサイズに対応した網目構造を構築することで、既存の石油化学製品とは異なる環境影響が非常に小さな、タンパク質性素材に結合する有害物質を除去可能で安全な吸着素材を開発することを目指す。

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Class subject

  • 基礎科学実習

    2023.12 - 2024.2   Winter quarter

  • 自然科学総合実験

    2023.10 - 2023.12   Fall quarter

  • 基幹教育セミナー

    2023.6 - 2023.8   Summer quarter

  • 自然科学総合実験

    2023.4 - 2023.6   Spring quarter

  • 基礎科学実習

    2022.12 - 2023.2   Winter quarter

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FD Participation

  • 2018.9   Role:Participation   Title:FD講演会「理系大学院・学部の教育改革を先進事例に学ぶ」

    Organizer:[Undergraduate school/graduate school/graduate faculty]

  • 2015.3   Role:Participation   Title:全学FD「障害学生支援におけるバリアフリー ~合理的配慮をめぐって~」

    Organizer:University-wide

  • 2015.2   Role:Participation   Title:基幹教育院FD

    Organizer:[Undergraduate school/graduate school/graduate faculty]

  • 2014.11   Role:Participation   Title:自殺対策FD

    Organizer:University-wide

  • 2014.9   Role:Participation   Title:基幹教育院FD

    Organizer:[Undergraduate school/graduate school/graduate faculty]

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Other educational activity and Special note

  • 2023  Class Teacher 

  • 2022  Class Teacher 

  • 2021  Class Teacher 

  • 2020  Class Teacher 

  • 2018  Class Teacher 

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