{"insert":{"user_id":"1000028663","type":"misc"},"force":{"see_also":[{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=385406","label":"url"}],"paper_title":{"en":"Advances in Preparation of Peptide and Protein Thioesters Aiming to Use in Medicinal Sciences","ja":"Advances in Preparation of Peptide and Protein Thioesters Aiming to Use in Medicinal Sciences"},"authors":{"en":[{"name":"Denda Masaya"},{"name":"Otaka Akira"}],"ja":[{"name":"傳田 将也"},{"name":"大髙 章"}]},"publication_date":"2022-05-09","publication_name":{"en":"Chemical & Pharmaceutical Bulletin","ja":"Chemical & Pharmaceutical Bulletin"},"volume":"Vol.70","number":"No.5","starting_page":"316","ending_page":"323","languages":["eng"],"invited":true,"identifiers":{"doi":["10.1248/cpb.c21-01019"],"issn":["1347-5223"]},"misc_type":"introduction_scientific_journal"}}
{"insert":{"user_id":"1000028663","type":"misc"},"force":{"see_also":[{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=381834","label":"url"}],"paper_title":{"en":"有機化学的視点からの標的タンパク質精製・機能解明ツールの開発","ja":"有機化学的視点からの標的タンパク質精製・機能解明ツールの開発"},"authors":{"en":[{"name":"Shigenaga Akira"},{"name":"Otaka Akira"}],"ja":[{"name":"重永 章"},{"name":"大髙 章"}]},"publication_date":"2019-12-25","publication_name":{"en":"Seikagaku","ja":"生化学"},"volume":"Vol.91","number":"No.6","starting_page":"795","ending_page":"799","languages":["jpn"],"invited":true,"identifiers":{"doi":["10.14952/SEIKAGAKU.2019.910795"],"issn":["2189-0544"]},"misc_type":"introduction_scientific_journal"}}
{"insert":{"user_id":"1000028663","type":"misc"},"force":{"see_also":[{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=340373","label":"url"}],"paper_title":{"en":"弁証法的薬学教育観-薬学における有機化学教育を考える-","ja":"弁証法的薬学教育観-薬学における有機化学教育を考える-"},"authors":{"en":[{"name":"Otaka Akira"}],"ja":[{"name":"大髙 章"}]},"publication_date":"2018-07-01","publication_name":{"en":"Journal of Synthetic Organic Chemistry, Japan","ja":"有機合成化学協会誌"},"volume":"Vol.76","number":"No.7","starting_page":"667","ending_page":"667","languages":["jpn"],"invited":true,"identifiers":{"doi":["10.5059/yukigoseikyokaishi.76.667"],"issn":["1883-6526"]},"misc_type":"introduction_scientific_journal"}}
{"insert":{"user_id":"1000028663","type":"misc"},"force":{"see_also":[{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=335853","label":"url"}],"paper_title":{"en":"十字路:Native Chemical Ligation法","ja":"十字路:Native Chemical Ligation法"},"authors":{"en":[{"name":"Otaka Akira"},{"name":"Shigenaga Akira"}],"ja":[{"name":"大髙 章"},{"name":"重永 章"}]},"publication_date":"2018-01-17","publication_name":{"en":"Journal of Synthetic Organic Chemistry, Japan","ja":"有機合成化学協会誌"},"volume":"Vol.76","number":"No.1","starting_page":"66","ending_page":"66","languages":["jpn"],"invited":true,"identifiers":{"doi":["10.5059/yukigoseikyokaishi.76.66"],"issn":["1883-6526"]},"misc_type":"introduction_scientific_journal"}}
{"insert":{"user_id":"1000028663","type":"misc"},"force":{"see_also":[{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=334220","label":"url"}],"paper_title":{"en":"天然に学ぶタンパク質合成化学","ja":"天然に学ぶタンパク質合成化学"},"authors":{"en":[{"name":"Otaka Akira"},{"name":"Shigenaga Akira"}],"ja":[{"name":"大髙 章"},{"name":"重永 章"}]},"publication_date":"2018-01-17","publication_name":{"en":"Journal of Synthetic Organic Chemistry, Japan","ja":"有機合成化学協会誌"},"volume":"Vol.76","number":"No.1","starting_page":"45","ending_page":"54","languages":["jpn"],"invited":true,"identifiers":{"doi":["10.5059/yukigoseikyokaishi.76.45"],"issn":["1883-6526"]},"misc_type":"introduction_scientific_journal"}}
{"insert":{"user_id":"1000028663","type":"misc"},"force":{"see_also":[{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=337578","label":"url"}],"paper_title":{"en":"第3章 第3節 ペプチドの不安定性を解決するペプチド結合の置換技術","ja":"第3章 第3節 ペプチドの不安定性を解決するペプチド結合の置換技術"},"authors":{"en":[{"name":"鳴海 哲夫"},{"name":"Otaka Akira"}],"ja":[{"name":"鳴海 哲夫"},{"name":"大髙 章"}]},"publication_date":"2017-12-17","publication_name":{"en":"ペプチド医薬品のスクリーニング・安定化・製剤化技術","ja":"ペプチド医薬品のスクリーニング・安定化・製剤化技術"},"starting_page":"130","ending_page":"140","languages":["jpn"],"invited":true,"misc_type":"introduction_scientific_journal"}}
{"insert":{"user_id":"1000028663","type":"misc"},"force":{"see_also":[{"@id":"https://repo.lib.tokushima-u.ac.jp/ja/111930","label":"url"},{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/28105728","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=321741","label":"url"}],"paper_title":{"en":"Invention of stimulus-responsive peptide-bond-cleaving residue (Spr) and its application to chemical biology tools","ja":"Invention of stimulus-responsive peptide-bond-cleaving residue (Spr) and its application to chemical biology tools"},"authors":{"en":[{"name":"Shigenaga Akira"},{"name":"Yamamoto Jun"},{"name":"Kohiki Taiki"},{"name":"Inokuma Tsubasa"},{"name":"Otaka Akira"}],"ja":[{"name":"重永 章"},{"name":"山本 純"},{"name":"古曳 泰規"},{"name":"猪熊 翼"},{"name":"大髙 章"}]},"description":{"en":"Elucidation of biological functions of peptides and proteins is essential for understanding peptide/protein-related biological events and developing drugs. Caged peptides and proteins that release a parent active peptide/protein by photo-irradiation have successfully been employed to elucidate the functions. Whereas the usual caged peptide/protein enables conversion of an inactive form to an active form (OFF-to-ON conversion) by photo-induced deprotection, photo-triggered main chain cleavage is reported to be applicable to ON-to-OFF conversion. These peptides and proteins are photo-responsive; however, if peptides and proteins could respond to other stimuli such as disease-related environment or enzymes, their range of application should be widened. To convert the photo-responsive peptide/protein into other stimulus-responsive peptide/protein, quite laborious de novo design and synthesis of the stimulus-responsive unit are required. In this context, we designed a stimulus-responsive peptide-bond-cleaving residue (Spr) in which the stimuli available for the main chain cleavage vary according to the choice of protecting groups on the residue. In this review, design and synthesis of Spr are introduced, and challenges to apply Spr to other fields to enable, for example, functional control, localization control, delivery of cargos, labeling of a protein of interest in living cells, and identification of target proteins of bioactive ligands are discussed. Copyright © 2017 European Peptide Society and John Wiley & Sons, Ltd.","ja":"Elucidation of biological functions of peptides and proteins is essential for understanding peptide/protein-related biological events and developing drugs. Caged peptides and proteins that release a parent active peptide/protein by photo-irradiation have successfully been employed to elucidate the functions. Whereas the usual caged peptide/protein enables conversion of an inactive form to an active form (OFF-to-ON conversion) by photo-induced deprotection, photo-triggered main chain cleavage is reported to be applicable to ON-to-OFF conversion. These peptides and proteins are photo-responsive; however, if peptides and proteins could respond to other stimuli such as disease-related environment or enzymes, their range of application should be widened. To convert the photo-responsive peptide/protein into other stimulus-responsive peptide/protein, quite laborious de novo design and synthesis of the stimulus-responsive unit are required. In this context, we designed a stimulus-responsive peptide-bond-cleaving residue (Spr) in which the stimuli available for the main chain cleavage vary according to the choice of protecting groups on the residue. In this review, design and synthesis of Spr are introduced, and challenges to apply Spr to other fields to enable, for example, functional control, localization control, delivery of cargos, labeling of a protein of interest in living cells, and identification of target proteins of bioactive ligands are discussed. Copyright © 2017 European Peptide Society and John Wiley & Sons, Ltd."},"publication_date":"2017-08-08","publication_name":{"en":"Journal of Peptide Science","ja":"Journal of Peptide Science"},"volume":"Vol.23","starting_page":"505","ending_page":"513","languages":["eng"],"invited":true,"identifiers":{"doi":["10.1002/psc.2961"],"issn":["1099-1387"]},"misc_type":"introduction_scientific_journal"}}
{"insert":{"user_id":"1000028663","type":"misc"},"force":{"see_also":[{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=313527","label":"url"}],"paper_title":{"en":"天然アミノ酸配列に適用可能な新規タンパク質チオエステル合成法の開発","ja":"天然アミノ酸配列に適用可能な新規タンパク質チオエステル合成法の開発"},"authors":{"en":[{"name":"Tsuda Yusuke"},{"name":"Shigenaga Akira"},{"name":"Satou Kouhei"},{"name":"Nakamura Takahiro"},{"name":"Kitakaze Keisuke"},{"name":"Inokuma Tsubasa"},{"name":"Itou Kouji"},{"name":"Otaka Akira"}],"ja":[{"name":"津田 雄介"},{"name":"重永 章"},{"name":"佐藤 浩平"},{"name":"中村 太寛"},{"name":"北風 圭介"},{"name":"猪熊 翼"},{"name":"伊藤 孝司"},{"name":"大髙 章"}]},"publication_date":"2016-06-08","publication_name":{"en":"ケミカルバイオロジー","ja":"ケミカルバイオロジー"},"volume":"Vol.9","starting_page":"7","ending_page":"10","languages":["jpn"],"invited":true,"misc_type":"introduction_scientific_journal"}}
{"insert":{"user_id":"1000028663","type":"misc"},"force":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/25467538","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=289415","label":"url"}],"paper_title":{"en":"Chemical synthesis of proteins using N-sulfanylethylanilide peptides, based on N-S acyl transfer chemistry","ja":"Chemical synthesis of proteins using N-sulfanylethylanilide peptides, based on N-S acyl transfer chemistry"},"authors":{"en":[{"name":"Otaka Akira"},{"name":"Sato Kohei"},{"name":"Shigenaga Akira"}],"ja":[{"name":"大髙 章"},{"name":"佐藤 浩平"},{"name":"重永 章"}]},"description":{"en":"Native chemical ligation (NCL), which features the use of peptide thioesters, is among the most reliable ligation protocols in chemical protein synthesis. Thioesters have conventionally been synthesized using tert-butyloxycarbonyl (Boc)-based solid-phase peptide synthesis (SPPS); however, the increasing use of 9-fluorenylmethyloxycarbonyl (Fmoc) SPPS requires an efficient preparative protocol for thioesters which is fully compatible with Fmoc chemistry. We have addressed this issue by mimicking the naturally occurring thioester-forming step seen in intein-mediated protein splicing of the intein-extein system, using an appropriate chemical device to induce N-S acyl transfer reaction, avoiding the problems associated with Fmoc strategies. We have developed N-sulfanylethylanilide (SEAlide) peptides, which can be synthesized by standard Fmoc SPPS and converted to the corresponding thioesters through treatment under acidic conditions. Extensive examination of SEAlide peptides showed that the amide-type SEAlide peptides can be directly and efficiently involved in NCL via thioester species in the presence of phosphate salts, even under neutral conditions. The presence or absence of phosphate salts provided kinetically controllable chemoselectivity in NCL for SEAlide peptides. This allowed SEAlide peptides to be used in both one-pot/N-to-C-directed sequential NCL under kinetically controlled conditions, and the convergent coupling of large peptide fragments, which facilitated the chemical synthesis of proteins over about 100 residues. The use of SEAlide peptides, enabling sequential NCL operated under kinetically controlled conditions, and the convergent coupling, were used for the total chemical synthesis of a 162-residue monoglycosylated GM2-activator protein (GM2AP) analog.","ja":"Native chemical ligation (NCL), which features the use of peptide thioesters, is among the most reliable ligation protocols in chemical protein synthesis. Thioesters have conventionally been synthesized using tert-butyloxycarbonyl (Boc)-based solid-phase peptide synthesis (SPPS); however, the increasing use of 9-fluorenylmethyloxycarbonyl (Fmoc) SPPS requires an efficient preparative protocol for thioesters which is fully compatible with Fmoc chemistry. We have addressed this issue by mimicking the naturally occurring thioester-forming step seen in intein-mediated protein splicing of the intein-extein system, using an appropriate chemical device to induce N-S acyl transfer reaction, avoiding the problems associated with Fmoc strategies. We have developed N-sulfanylethylanilide (SEAlide) peptides, which can be synthesized by standard Fmoc SPPS and converted to the corresponding thioesters through treatment under acidic conditions. Extensive examination of SEAlide peptides showed that the amide-type SEAlide peptides can be directly and efficiently involved in NCL via thioester species in the presence of phosphate salts, even under neutral conditions. The presence or absence of phosphate salts provided kinetically controllable chemoselectivity in NCL for SEAlide peptides. This allowed SEAlide peptides to be used in both one-pot/N-to-C-directed sequential NCL under kinetically controlled conditions, and the convergent coupling of large peptide fragments, which facilitated the chemical synthesis of proteins over about 100 residues. The use of SEAlide peptides, enabling sequential NCL operated under kinetically controlled conditions, and the convergent coupling, were used for the total chemical synthesis of a 162-residue monoglycosylated GM2-activator protein (GM2AP) analog."},"publication_date":"2015-05-16","publication_name":{"en":"Topics in Current Chemistry","ja":"Topics in Current Chemistry"},"volume":"Vol.363","starting_page":"33","ending_page":"56","languages":["eng"],"invited":true,"identifiers":{"doi":["10.1007/128_2014_586"],"issn":["0340-1022"]},"misc_type":"introduction_scientific_journal"}}
{"insert":{"user_id":"1000028663","type":"misc"},"force":{"see_also":[{"@id":"https://cir.nii.ac.jp/crid/1521417754728344960/","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=301991","label":"url"}],"paper_title":{"en":"タンパク性医薬品開発に向けたペプチド化学","ja":"タンパク性医薬品開発に向けたペプチド化学"},"authors":{"en":[{"name":"Nakamura Takahiro"},{"name":"Satou Kouhei"},{"name":"Otaka Akira"}],"ja":[{"name":"中村 太寛"},{"name":"佐藤 浩平"},{"name":"大髙 章"}]},"publication_date":"2014-11","publication_name":{"en":"化学工業(特集 ペプチド化学の新潮流(1))","ja":"化学工業(特集 ペプチド化学の新潮流(1))"},"volume":"Vol.65","number":"No.11","starting_page":"842","ending_page":"848","languages":["jpn"],"invited":true,"identifiers":{"issn":["0451-2014"]},"misc_type":"introduction_scientific_journal"}}
{"insert":{"user_id":"1000028663","type":"misc"},"force":{"see_also":[{"@id":"http://repo.lib.tokushima-u.ac.jp/111953","label":"url"},{"@id":"https://repo.lib.tokushima-u.ac.jp/ja/111953","label":"url"},{"@id":"https://cir.nii.ac.jp/crid/1050564287420872448/","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=287772","label":"url"}],"paper_title":{"en":"Development of Stimulus-responsive Amino Acids that are Potentially Applicable to Chemical Biology Use","ja":"刺激応答型アミノ酸の開発と生命科学分野への展開"},"authors":{"en":[{"name":"Shigenaga Akira"},{"name":"Otaka Akira"}],"ja":[{"name":"重永 章"},{"name":"大髙 章"}]},"publication_date":"2014-11","publication_name":{"en":"化学工業(特集 ペプチド化学の新潮流(1))","ja":"化学工業(特集 ペプチド化学の新潮流(1))"},"volume":"Vol.65","number":"No.11","starting_page":"849","ending_page":"856","languages":["jpn"],"invited":true,"identifiers":{"issn":["0451-2014"]},"misc_type":"introduction_scientific_journal"}}
{"insert":{"user_id":"1000028663","type":"misc"},"force":{"see_also":[{"@id":"https://ci.nii.ac.jp/naid/40020104679/","label":"url"},{"@id":"https://cir.nii.ac.jp/crid/1521136280904574080/","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=285198","label":"url"}],"paper_title":{"en":"Development of Chemical Platform for Peptide/Protein-based Drug Discovery","ja":"ペプチド・タンパク質を基盤とする創薬展開への化学基盤の開拓"},"authors":{"en":[{"name":"Sato Kohei"},{"name":"Otaka Akira"}],"ja":[{"name":"佐藤 浩平"},{"name":"大髙 章"}]},"publication_date":"2014-06-16","publication_name":{"en":"Chemical Industry","ja":"化学工業"},"volume":"Vol.65","number":"No.6","starting_page":"411","ending_page":"417","languages":["jpn"],"identifiers":{"issn":["0451-2014"]},"misc_type":"introduction_scientific_journal"}}
{"insert":{"user_id":"1000028663","type":"misc"},"force":{"see_also":[{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=263134","label":"url"}],"paper_title":{"en":"新規タンパク質選択的ラベル化試薬''SEAL-tag''の開発研究","ja":"新規タンパク質選択的ラベル化試薬''SEAL-tag''の開発研究"},"authors":{"en":[{"name":"Denda Masaya"},{"name":"Yamamoto Jun"},{"name":"Satou Kouhei"},{"name":"Sakamoto Ken"},{"name":"Shigenaga Akira"},{"name":"Sato Youichi"},{"name":"Yoshimura Yoshiyuki"},{"name":"Yamauchi Aiko"},{"name":"Otaka Akira"}],"ja":[{"name":"傳田 将也"},{"name":"山本 純"},{"name":"佐藤 浩平"},{"name":"坂本 健"},{"name":"重永 章"},{"name":"佐藤 陽一"},{"name":"吉村 好之"},{"name":"山内 あい子"},{"name":"大髙 章"}]},"publication_date":"2013-06-10","publication_name":{"en":"ケミカルバイオロジー","ja":"ケミカルバイオロジー"},"volume":"Vol.6","starting_page":"6","ending_page":"9","languages":["jpn"],"invited":true,"misc_type":"introduction_scientific_journal"}}
{"insert":{"user_id":"1000028663","type":"misc"},"force":{"see_also":[{"@id":"http://ci.nii.ac.jp/naid/10031124010/","label":"url"},{"@id":"https://cir.nii.ac.jp/crid/1390282680316668032/","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=257809","label":"url"}],"paper_title":{"en":"Development of Organic and Bio-organic Methodologies for the Synthesis of Proteins","ja":"情報発信型人工タンパク質創製に向けた有機・生物有機化学的挑戦"},"authors":{"en":[{"name":"Otaka Akira"}],"ja":[{"name":"大髙 章"}]},"description":{"en":"Functional analyses of endogenous proteins represent indispensable steps for development of drugs for the protein targets. Here, informative-function-incorporated artificial proteins corresponding to the targets should serve as a useful molecular device for evaluating the naturally occurring proteins as a potential drug target. Chemical synthesis and chemical manipulation of proteins allow such artificial proteins to be prepared. We therefore developed a facile synthetic protocol for proteins and a chemical device for functional change of proteins. In this review are addressed both N-sulfanylethylanilide (SEAlide) peptides for protein synthesis and stimulus-responsive amino acids for the functional conversion. SEAlide peptides were initially developed as peptide thioester precursors obtainable by 9-fluorenylmethyloxycarbonyl (Fmoc) solid-phase peptide synthesis. Investigation on the SEAlide peptides uncovered that a one-pot/multi-fragment sequential native chemical ligation (NCL) is achieved efficiently using the SEAlide unit to give proteins. For functional change of proteins, stimulus-responsive amino acids were developed. Upon responding to various stimuli, the newly developed amino acid-containing peptides are spliced into two peptide parts. Combination of the splicing reaction and an acyl-transfer chemistry allows the function of peptide to be changed.","ja":"Functional analyses of endogenous proteins represent indispensable steps for development of drugs for the protein targets. Here, informative-function-incorporated artificial proteins corresponding to the targets should serve as a useful molecular device for evaluating the naturally occurring proteins as a potential drug target. Chemical synthesis and chemical manipulation of proteins allow such artificial proteins to be prepared. We therefore developed a facile synthetic protocol for proteins and a chemical device for functional change of proteins. In this review are addressed both N-sulfanylethylanilide (SEAlide) peptides for protein synthesis and stimulus-responsive amino acids for the functional conversion. SEAlide peptides were initially developed as peptide thioester precursors obtainable by 9-fluorenylmethyloxycarbonyl (Fmoc) solid-phase peptide synthesis. Investigation on the SEAlide peptides uncovered that a one-pot/multi-fragment sequential native chemical ligation (NCL) is achieved efficiently using the SEAlide unit to give proteins. For functional change of proteins, stimulus-responsive amino acids were developed. Upon responding to various stimuli, the newly developed amino acid-containing peptides are spliced into two peptide parts. Combination of the splicing reaction and an acyl-transfer chemistry allows the function of peptide to be changed."},"publication_date":"2012-10-01","publication_name":{"en":"Journal of Synthetic Organic Chemistry, Japan","ja":"有機合成化学協会誌"},"volume":"Vol.70","number":"No.10","starting_page":"1054","ending_page":"1054","languages":["jpn"],"invited":true,"identifiers":{"doi":["10.5059/yukigoseikyokaishi.70.1054"],"issn":["0037-9980"]},"misc_type":"introduction_scientific_journal"}}
{"insert":{"user_id":"1000028663","type":"misc"},"force":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/22927228","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=257821","label":"url"}],"paper_title":{"en":"One-pot/sequential native chemical ligation using N-sulfanylethylanilide peptide","ja":"One-pot/sequential native chemical ligation using N-sulfanylethylanilide peptide"},"authors":{"en":[{"name":"Otaka Akira"},{"name":"Sato Kohei"},{"name":"Ding Hao"},{"name":"Shigenaga Akira"}],"ja":[{"name":"大髙 章"},{"name":"佐藤 浩平"},{"name":"丁 昊"},{"name":"重永 章"}]},"description":{"en":"N-Sulfanylethylanilide (SEAlide) peptides were developed with the aim of achieving facile synthesis of peptide thioesters by 9-fluorenylmethyloxycarbonyl (Fmoc)-based solid-phase peptide synthesis (Fmoc SPPS). Initially, SEAlide peptides were found to be converted to the corresponding peptide thioesters under acidic conditions. However, the SEAlide moiety was proved to function as a thioester in the presence of phosphate salts and to participate in native chemical ligation (NCL) with N-terminal cysteinyl peptides, and this has served as a powerful protein synthesis methodology. The reactivity of a SEAlide peptide (anilide vs. thioester) can be easily tuned with or without the use of phosphate salts. This interesting property of SEAlide peptides allows sequential three-fragment or unprecedented four-fragment ligation for efficient one-pot peptide/protein synthesis. Furthermore, dual-kinetically controlled ligation, which enables three peptide fragments simultaneously present in the reaction to be ligated in the correct order, was first achieved using a SEAlide peptide. Beyond our initial expectations, SEAlide peptides have served in protein chemistry fields as very useful crypto-peptide thioesters.","ja":"N-Sulfanylethylanilide (SEAlide) peptides were developed with the aim of achieving facile synthesis of peptide thioesters by 9-fluorenylmethyloxycarbonyl (Fmoc)-based solid-phase peptide synthesis (Fmoc SPPS). Initially, SEAlide peptides were found to be converted to the corresponding peptide thioesters under acidic conditions. However, the SEAlide moiety was proved to function as a thioester in the presence of phosphate salts and to participate in native chemical ligation (NCL) with N-terminal cysteinyl peptides, and this has served as a powerful protein synthesis methodology. The reactivity of a SEAlide peptide (anilide vs. thioester) can be easily tuned with or without the use of phosphate salts. This interesting property of SEAlide peptides allows sequential three-fragment or unprecedented four-fragment ligation for efficient one-pot peptide/protein synthesis. Furthermore, dual-kinetically controlled ligation, which enables three peptide fragments simultaneously present in the reaction to be ligated in the correct order, was first achieved using a SEAlide peptide. Beyond our initial expectations, SEAlide peptides have served in protein chemistry fields as very useful crypto-peptide thioesters."},"publication_date":"2012-08-23","publication_name":{"en":"Chemical Record","ja":"Chemical Record"},"volume":"Vol.12","number":"No.5","starting_page":"479","ending_page":"490","languages":["eng"],"invited":true,"identifiers":{"doi":["10.1002/tcr.201200007"],"issn":["1528-0691"]},"misc_type":"introduction_scientific_journal"}}
{"insert":{"user_id":"1000028663","type":"misc"},"force":{"see_also":[{"@id":"http://ci.nii.ac.jp/naid/10026870593/","label":"url"},{"@id":"https://cir.nii.ac.jp/crid/1390001205312881408/","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=214199","label":"url"}],"paper_title":{"en":"Recent Progress in the Synthetic Methodologies of Peptide Thioesters","ja":"ペプチドチオエステル合成法の最近の進展"},"authors":{"en":[{"name":"Shigenaga Akira"},{"name":"Sato Kohei"},{"name":"Otaka Akira"}],"ja":[{"name":"重永 章"},{"name":"佐藤 浩平"},{"name":"大髙 章"}]},"description":{"en":"Investigations of biological processes by using peptide, protein, or its derivative are undoubtedly valuable. In this field, chemical synthesis of native or modified peptides/proteins is indispensable. Fragment condensation strategy, such as thioester method or native chemical ligation, is widely used for chemical synthesis of large peptides and proteins. C-Terminal peptide/protein thioesters have been used as building blocks for the fragment condensation strategy. Therefore, development of methodologies for preparing C-terminal peptide/protein thioesters is one of the most attracting theme in recent peptide/protein chemistry field. In this review, the methodologies for preparing C-terminal peptide/protein thioesters utilizing chemistry, biochemistry, or gene engineering are summarized.","ja":"Investigations of biological processes by using peptide, protein, or its derivative are undoubtedly valuable. In this field, chemical synthesis of native or modified peptides/proteins is indispensable. Fragment condensation strategy, such as thioester method or native chemical ligation, is widely used for chemical synthesis of large peptides and proteins. C-Terminal peptide/protein thioesters have been used as building blocks for the fragment condensation strategy. Therefore, development of methodologies for preparing C-terminal peptide/protein thioesters is one of the most attracting theme in recent peptide/protein chemistry field. In this review, the methodologies for preparing C-terminal peptide/protein thioesters utilizing chemistry, biochemistry, or gene engineering are summarized."},"publication_date":"2010-09-01","publication_name":{"en":"Journal of Synthetic Organic Chemistry, Japan","ja":"有機合成化学協会誌"},"volume":"Vol.68","number":"No.9","starting_page":"911","ending_page":"919","languages":["jpn"],"identifiers":{"doi":["10.5059/yukigoseikyokaishi.68.911"],"issn":["0037-9980"]},"misc_type":"introduction_scientific_journal"}}
{"insert":{"user_id":"1000028663","type":"misc"},"force":{"see_also":[{"@id":"http://ci.nii.ac.jp/naid/130000451315/","label":"url"},{"@id":"https://cir.nii.ac.jp/crid/1390282680287568896/","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=214200","label":"url"}],"paper_title":{"en":"十字路:セーフティーキャッチリンカー","ja":"十字路:セーフティーキャッチリンカー"},"authors":{"en":[{"name":"Shigenaga Akira"},{"name":"Sato Kohei"},{"name":"Otaka Akira"}],"ja":[{"name":"重永 章"},{"name":"佐藤 浩平"},{"name":"大髙 章"}]},"publication_date":"2010-09","publication_name":{"en":"Journal of Synthetic Organic Chemistry, Japan","ja":"有機合成化学協会誌"},"volume":"Vol.68","number":"No.9","starting_page":"973","ending_page":"973","languages":["jpn"],"invited":true,"identifiers":{"doi":["10.5059/yukigoseikyokaishi.68.973"],"issn":["0037-9980"]},"misc_type":"introduction_scientific_journal"}}
{"insert":{"user_id":"1000028663","type":"misc"},"force":{"see_also":[{"@id":"https://repo.lib.tokushima-u.ac.jp/ja/116114","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=190341","label":"url"}],"paper_title":{"en":"磁気浮上を利用した簡便な固相反応モニター法の開発","ja":"磁気浮上を利用した簡便な固相反応モニター法の開発"},"authors":{"en":[{"name":"Shigenaga Akira"},{"name":"Otaka Akira"}],"ja":[{"name":"重永 章"},{"name":"大髙 章"}]},"publication_date":"2009-05","publication_name":{"en":"Chemical Biology","ja":"ケミカルバイオロジー"},"volume":"Vol.2","starting_page":"13","ending_page":"13","languages":["jpn"],"misc_type":"introduction_scientific_journal"}}
{"insert":{"user_id":"1000028663","type":"misc"},"force":{"see_also":[{"@id":"http://ci.nii.ac.jp/naid/10024278609/","label":"url"},{"@id":"https://cir.nii.ac.jp/crid/1390282680288398720/","label":"url"},{"@id":"https://www.scopus.com/record/display.url?eid=2-s2.0-57049119193&origin=inward","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=303147","label":"url"}],"paper_title":{"en":"Synthesis of Highly Functionalized Alkene Dipeptide Isosteres and Its Application to the Structure-Activity Relationship Study on Bioactive Peptides","ja":"アルケン型ジペプチドイソスターの合成法の開発と生理活性ペプチドの構造活性相関研究への応用"},"authors":{"en":[{"name":"大石 真也"},{"name":"鳴海 哲夫"},{"name":"大野 浩章"},{"name":"Otaka Akira"},{"name":"藤井 信孝"}],"ja":[{"name":"大石 真也"},{"name":"鳴海 哲夫"},{"name":"大野 浩章"},{"name":"大髙 章"},{"name":"藤井 信孝"}]},"description":{"en":"Peptide bonds are one of the essential contributors to overall structure and functions of bioactive peptides. The partial double-bond character derived from the resonance structure restricts the free rotation of the carbon-nitrogen bond and stabilizes the planar conformations. Additionally, the ability to form hydrogen bonds allows the stabilization of characteristic secondary structures such as α-helix and β-turn as well as the association with the receptors. Alkene dipeptide isosteres, based on the concept of ω-dihedral angle planarity, have been used as amide bond equivalents, which serve as mechanistic probes lacking amide polarity. We have developed a facile methodology for the stereoselective synthesis of highly functional dipeptide isosteres. The key reaction is the alkylation of δ-aminated α, β-enoates having an appropriate leaving group at the γ-position. Organocopper-mediated anti-SN2' alkylation of α, β-enoates afforded multi-substituted olefin-containing isosteres. One-pot reduction-transmetalation-alkylation of γ, γ-difluoro-α, β-enoates provided fluoroalkene dipeptide isosteres. Reduction of these substrates with organocuprate, SmI2, or Pd/PhSiH3/Et3N system gave Xaa-Gly-type mimetics. Similar methods were also utilized for the preparation of cis-peptide bond mimetics. The resulting isosteres and the key intermediates were studied in structure-activity relationship of bioactive peptides including integrin αvβ3 antagonist, chemokine receptor CXCR 4 antagonist, puberty-related GPR 54 agonist, and peptide transporter PEPT1 substrate.","ja":"Peptide bonds are one of the essential contributors to overall structure and functions of bioactive peptides. The partial double-bond character derived from the resonance structure restricts the free rotation of the carbon-nitrogen bond and stabilizes the planar conformations. Additionally, the ability to form hydrogen bonds allows the stabilization of characteristic secondary structures such as α-helix and β-turn as well as the association with the receptors. Alkene dipeptide isosteres, based on the concept of ω-dihedral angle planarity, have been used as amide bond equivalents, which serve as mechanistic probes lacking amide polarity. We have developed a facile methodology for the stereoselective synthesis of highly functional dipeptide isosteres. The key reaction is the alkylation of δ-aminated α, β-enoates having an appropriate leaving group at the γ-position. Organocopper-mediated anti-SN2' alkylation of α, β-enoates afforded multi-substituted olefin-containing isosteres. One-pot reduction-transmetalation-alkylation of γ, γ-difluoro-α, β-enoates provided fluoroalkene dipeptide isosteres. Reduction of these substrates with organocuprate, SmI2, or Pd/PhSiH3/Et3N system gave Xaa-Gly-type mimetics. Similar methods were also utilized for the preparation of cis-peptide bond mimetics. The resulting isosteres and the key intermediates were studied in structure-activity relationship of bioactive peptides including integrin αvβ3 antagonist, chemokine receptor CXCR 4 antagonist, puberty-related GPR 54 agonist, and peptide transporter PEPT1 substrate."},"publication_date":"2008-09-01","publication_name":{"en":"Journal of Synthetic Organic Chemistry, Japan","ja":"有機合成化学協会誌"},"volume":"Vol.66","number":"No.9","starting_page":"846","ending_page":"857","languages":["jpn"],"invited":true,"identifiers":{"doi":["10.5059/yukigoseikyokaishi.66.846"],"issn":["0037-9980"]},"misc_type":"introduction_scientific_journal"}}
{"insert":{"user_id":"1000028663","type":"misc"},"force":{"see_also":[{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=175800","label":"url"}],"paper_title":{"en":"刺激応答型アミノ酸を利用した核-細胞質シャトルペプチドの開発","ja":"刺激応答型アミノ酸を利用した核-細胞質シャトルペプチドの開発"},"authors":{"en":[{"name":"Shigenaga Akira"},{"name":"Tsuji Daisuke"},{"name":"Nishioka Naomi"},{"name":"Tsuda Shugo"},{"name":"Itou Kouji"},{"name":"Otaka Akira"}],"ja":[{"name":"重永 章"},{"name":"辻 大輔"},{"name":"西岡 直美"},{"name":"津田 修吾"},{"name":"伊藤 孝司"},{"name":"大髙 章"}]},"publication_date":"2008-05","publication_name":{"en":"Chemical Biology","ja":"ケミカルバイオロジー"},"volume":"Vol.1","number":"No.1","starting_page":"7","ending_page":"10","languages":["jpn"],"misc_type":"introduction_scientific_journal"}}
{"insert":{"user_id":"1000028663","type":"misc"},"force":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/18051429","label":"url"},{"@id":"https://www.scopus.com/record/display.url?eid=2-s2.0-38449088482&origin=inward","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=165649","label":"url"}],"paper_title":{"en":"[New type of synthetic peptide library for identifying ligand-binding activity].","ja":"Split and Pool法を用いたOne-bead, One-peptideライブラリーの構築とハイスループットスクリーニングへの展開"},"authors":{"en":[{"name":"Shigenaga Akira"},{"name":"Otaka Akira"}],"ja":[{"name":"重永 章"},{"name":"大髙 章"}]},"publication_date":"2007-10","publication_name":{"en":"Tanpakushitsu Kakusan Koso","ja":"蛋白質 核酸 酵素"},"volume":"Vol.52","number":"No.13 Suppl","starting_page":"1792","ending_page":"1793","languages":["jpn"],"identifiers":{"issn":["0039-9450"]},"misc_type":"introduction_scientific_journal"}}
{"insert":{"user_id":"1000028663","type":"misc"},"force":{"see_also":[{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=303254","label":"url"}],"paper_title":{"en":"プロテオミクスを基盤とするケミカルバイオロジー -情報から制御へ","ja":"プロテオミクスを基盤とするケミカルバイオロジー -情報から制御へ"},"authors":{"en":[{"name":"藤井 信孝"},{"name":"大石 真也"},{"name":"Otaka Akira"}],"ja":[{"name":"藤井 信孝"},{"name":"大石 真也"},{"name":"大髙 章"}]},"publication_date":"2006-10","publication_name":{"en":"Bionics","ja":"Bionics"},"volume":"Vol.3","number":"No.10","starting_page":"46","ending_page":"51","languages":["jpn"],"invited":true,"misc_type":"introduction_scientific_journal"}}
{"insert":{"user_id":"1000028663","type":"misc"},"force":{"see_also":[{"@id":"https://ci.nii.ac.jp/naid/40007473491/","label":"url"},{"@id":"https://cir.nii.ac.jp/crid/1523106604538391680/","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=303250","label":"url"}],"paper_title":{"en":"膜融合阻害性抗ウイルスペプチドの開発","ja":"膜融合阻害性抗ウイルスペプチドの開発"},"authors":{"en":[{"name":"Otaka Akira"},{"name":"藤井 信孝"}],"ja":[{"name":"大髙 章"},{"name":"藤井 信孝"}]},"publication_date":"2006-10","publication_name":{"en":"Chemical Industry","ja":"化学工業"},"volume":"Vol.57","number":"No.10","starting_page":"797","ending_page":"801","languages":["jpn"],"invited":true,"identifiers":{"issn":["0451-2014"]},"misc_type":"introduction_scientific_journal"}}
{"insert":{"user_id":"1000028663","type":"misc"},"force":{"see_also":[{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=143877","label":"url"}],"paper_title":{"en":"ケミカルプロテオミックス先導型創薬基盤の革新","ja":"ケミカルプロテオミックス先導型創薬基盤の革新"},"authors":{"en":[{"name":"藤井 信孝"},{"name":"Otaka Akira"},{"name":"玉村 啓和"}],"ja":[{"name":"藤井 信孝"},{"name":"大髙 章"},{"name":"玉村 啓和"}]},"publication_date":"2005-11","publication_name":{"en":"細胞工学","ja":"細胞工学"},"volume":"Vol.15","number":"No.11","starting_page":"1181","ending_page":"1186","languages":["jpn"],"identifiers":{"issn":["0287-3796"]},"misc_type":"introduction_scientific_journal"}}
{"insert":{"user_id":"1000028663","type":"misc"},"force":{"see_also":[{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=143876","label":"url"}],"paper_title":{"en":"抗SARS-CoV活性ペプチドの創製研究","ja":"抗SARS-CoV活性ペプチドの創製研究"},"authors":{"en":[{"name":"西川 裕輝"},{"name":"藤井 信孝"},{"name":"Otaka Akira"}],"ja":[{"name":"西川 裕輝"},{"name":"藤井 信孝"},{"name":"大髙 章"}]},"publication_date":"2005","publication_name":{"en":"Med. Chem. News","ja":"Med. Chem. News"},"volume":"Vol.15","starting_page":"18","ending_page":"23","languages":["jpn"],"misc_type":"introduction_scientific_journal"}}
{"insert":{"user_id":"1000028663","type":"misc"},"force":{"see_also":[{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=143875","label":"url"}],"paper_title":{"en":"SARS治療薬の展望","ja":"SARS治療薬の展望"},"authors":{"en":[{"name":"Otaka Akira"},{"name":"藤井 信孝"},{"name":"山本 直樹"}],"ja":[{"name":"大髙 章"},{"name":"藤井 信孝"},{"name":"山本 直樹"}]},"publication_date":"2004-11","publication_name":{"en":"New Horizon for Medicine","ja":"現代医療"},"volume":"Vol.36","number":"No.11","starting_page":"64","ending_page":"51","languages":["jpn"],"identifiers":{"issn":["0533-7259"]},"misc_type":"introduction_scientific_journal"}}
{"insert":{"user_id":"1000028663","type":"misc"},"force":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/15054894","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=143860","label":"url"}],"paper_title":{"en":"Synthesis of fluorine-containing bioisosteres corresponding to phosphoamino acids and dipeptide units","ja":"Synthesis of fluorine-containing bioisosteres corresponding to phosphoamino acids and dipeptide units"},"authors":{"en":[{"name":"Otaka Akira"},{"name":"Mitsuyama Etsuko"},{"name":"Watanabe Junko"},{"name":"Watanabe Hideaki"},{"name":"Fujii Nobutaka"}],"ja":[{"name":"大髙 章"},{"name":"Mitsuyama Etsuko"},{"name":"Watanabe Junko"},{"name":"Watanabe Hideaki"},{"name":"Fujii Nobutaka"}]},"description":{"en":"It has been shown that fluorinated analogues of naturally occurring biological active compounds including amino acids often exhibit unique physiological activity. Among wide varieties of fluorine-containing amino acids, nonhydrolyzable phosphoamino acids possessing a substituent of the difluoromethylene (CF(2)) unit for the phosphoryl ester oxygen are of value in the medicinal and biological fields. We have engaged in the synthesis of these classes of nonhydrolyzable phosphoamino acids corresponding to pTyr 3, pSer 4, and pThr 5 with their incorporation into peptides using newly developed deprotecting procedures. In this article, stereoselective synthesis of the CF(2)-substituted pThr mimetics and development of a two-step deprotecting methodology for the nonhydrolyzable analogues are reviewed. In the course of the above synthetic study, we found that gamma,gamma-difluoro-alpha,beta-enoates were reduced to gamma-fluoro-beta,gamma-enoates by organocopper reagents and then applied to the synthesis of (Z)-fluoroalkene dipeptide isosteres, which have served as potential dipeptide mimetics having structural as well as electrostatic similarity to the parent peptide bonds. Furthermore, mechanistic investigation of the organocopper-mediated reduction led us to development of a SmI(2)-mediated approach toward the synthesis of the fluoroalkene isosteres.","ja":"It has been shown that fluorinated analogues of naturally occurring biological active compounds including amino acids often exhibit unique physiological activity. Among wide varieties of fluorine-containing amino acids, nonhydrolyzable phosphoamino acids possessing a substituent of the difluoromethylene (CF(2)) unit for the phosphoryl ester oxygen are of value in the medicinal and biological fields. We have engaged in the synthesis of these classes of nonhydrolyzable phosphoamino acids corresponding to pTyr 3, pSer 4, and pThr 5 with their incorporation into peptides using newly developed deprotecting procedures. In this article, stereoselective synthesis of the CF(2)-substituted pThr mimetics and development of a two-step deprotecting methodology for the nonhydrolyzable analogues are reviewed. In the course of the above synthetic study, we found that gamma,gamma-difluoro-alpha,beta-enoates were reduced to gamma-fluoro-beta,gamma-enoates by organocopper reagents and then applied to the synthesis of (Z)-fluoroalkene dipeptide isosteres, which have served as potential dipeptide mimetics having structural as well as electrostatic similarity to the parent peptide bonds. Furthermore, mechanistic investigation of the organocopper-mediated reduction led us to development of a SmI(2)-mediated approach toward the synthesis of the fluoroalkene isosteres."},"publication_date":"2004","publication_name":{"en":"Biopolymers","ja":"Biopolymers"},"volume":"Vol.76","number":"No.2","starting_page":"140","ending_page":"149","languages":["eng"],"identifiers":{"doi":["10.1002/bip.10570"],"issn":["0006-3525"]},"misc_type":"introduction_scientific_journal"}}
{"insert":{"user_id":"1000028663","type":"misc"},"force":{"see_also":[{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=143874","label":"url"}],"paper_title":{"en":"高付加価値ペプチド合成のための最終脱保護法の開発と細胞内情報伝達機構解明への展開研究","ja":"高付加価値ペプチド合成のための最終脱保護法の開発と細胞内情報伝達機構解明への展開研究"},"authors":{"en":[{"name":"Otaka Akira"}],"ja":[{"name":"大髙 章"}]},"publication_date":"2000","publication_name":{"en":"Journal of the Pharmaceutical Society of Japan","ja":"薬学雑誌"},"volume":"Vol.120","starting_page":"54","ending_page":"67","languages":["jpn"],"identifiers":{"issn":["0031-6903"]},"misc_type":"introduction_scientific_journal"}}
{"insert":{"user_id":"1000028663","type":"misc"},"force":{"see_also":[{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=143872","label":"url"}],"paper_title":{"en":"構造生物学の方法論の新しい展開 --- リン酸化ペプチドの化学合成","ja":"構造生物学の方法論の新しい展開 --- リン酸化ペプチドの化学合成"},"authors":{"en":[{"name":"Otaka Akira"},{"name":"相本 三郎"}],"ja":[{"name":"大髙 章"},{"name":"相本 三郎"}]},"publication_date":"1999","publication_name":{"en":"Tanpakushitsu Kakusan Koso","ja":"蛋白質 核酸 酵素"},"volume":"Vol.44","starting_page":"302","ending_page":"309","languages":["jpn"],"identifiers":{"issn":["0039-9450"]},"misc_type":"introduction_scientific_journal"}}
{"insert":{"user_id":"1000028663","type":"misc"},"force":{"see_also":[{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=143866","label":"url"}],"paper_title":{"en":"ジスルフィド結合形成材","ja":"ジスルフィド結合形成材"},"authors":{"en":[{"name":"Otaka Akira"},{"name":"藤井 信孝"}],"ja":[{"name":"大髙 章"},{"name":"藤井 信孝"}]},"publication_date":"1990-11","publication_name":{"en":"有機合成化学協会誌","ja":"有機合成化学協会誌"},"volume":"Vol.48","starting_page":"1010","ending_page":"1011","languages":["jpn"],"misc_type":"introduction_scientific_journal"}}
{"insert":{"user_id":"1000028663","type":"misc"},"force":{"see_also":[{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=143865","label":"url"}],"paper_title":{"en":"ペプチド合成における最終脱保護材","ja":"ペプチド合成における最終脱保護材"},"authors":{"en":[{"name":"Otaka Akira"},{"name":"藤井 信孝"}],"ja":[{"name":"大髙 章"},{"name":"藤井 信孝"}]},"publication_date":"1990-11","publication_name":{"en":"有機合成化学協会誌","ja":"有機合成化学協会誌"},"volume":"Vol.48","starting_page":"1044","ending_page":"1045","languages":["jpn"],"misc_type":"introduction_scientific_journal"}}
{"insert":{"user_id":"1000028663","type":"misc"},"force":{"see_also":[{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=143862","label":"url"}],"paper_title":{"en":"シスチン含有ペプチドの新規合成法","ja":"シスチン含有ペプチドの新規合成法"},"authors":{"en":[{"name":"Otaka Akira"},{"name":"藤井 信孝"}],"ja":[{"name":"大髙 章"},{"name":"藤井 信孝"}]},"publication_date":"1990-07","publication_name":{"en":"有機合成化学協会誌","ja":"有機合成化学協会誌"},"volume":"Vol.48","starting_page":"658","ending_page":"671","languages":["jpn"],"misc_type":"introduction_scientific_journal"}}