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Molecular Design of Artificial Proteins Bearing Novel Structural Motif by Utilizing an Unnatural Amino Acid

Research Project

Project/Area Number 14380292
Research Category

Grant-in-Aid for Scientific Research (B)

Allocation TypeSingle-year Grants
Section一般
Research Field Bioorganic chemistry
Research InstitutionKitasato University

Principal Investigator

ISHIDA Hitoshi  Kitasato University, School of Science, Associate Professor, 理学部, 助教授 (30203003)

Co-Investigator(Kenkyū-buntansha) OISHI Shigero  Kitasato University, School of Science, Professor, 理学部, 教授 (80213619)
Project Period (FY) 2002 – 2004
Project Status Completed (Fiscal Year 2004)
Budget Amount *help
¥15,000,000 (Direct Cost: ¥15,000,000)
Fiscal Year 2004: ¥2,200,000 (Direct Cost: ¥2,200,000)
Fiscal Year 2003: ¥5,000,000 (Direct Cost: ¥5,000,000)
Fiscal Year 2002: ¥7,800,000 (Direct Cost: ¥7,800,000)
KeywordsArtificial Proteins / Unnatural Amino Acid / Peptide / Ruthenium / Bipyridine / Photochemical Property / Photo-function / Anion Binding / 光化学的声質 / CDスペクトル / アミド / アミド基 / 青色発光物質
Research Abstract

The purpose of this work is to design and synthesize artificial proteins, which consist of peptides containing an unnatural and coordinating amino acid, 5'-amino-2,2'-bipyridine-5-carboxylic acid. The peptides containing a couple of residues of the unnatural amino acid are expected to coordinate with a metal ion, affording the artificial proteins with unique structural motifs. In the synthesis of peptides, the dipeptide units, which were separately prepared, were introduced into the common solid phase synthetic methods ; otherwise the synthesis was difficult due to its less reactive amino group. The 21-mer peptides with three residues of the unnatural amino acids were successfully synthesized by the methodology. Furthermore, formation of the iron(II) complexes by reacting the peptides with iron(II) ion was observed in absorption spectra, showing Metal-to-Ligand Charge Transfer (MLCT) band at 541 nm. On the other hand, if ruthenium(II) ion was used, the artificial proteins had ruthenium tris(bipyridine) type complexes as the core, which were expected to appear photo-functions, such as emission, photo-catalytic, and photo-induced electron transfer abilities. Since there are, however, few works on ruthenium tris(5,5'-disubstitueted-2,2'-bipyridine) complexes, we synthesized various ruthenium complexes of the unnatural amino acid derivatives and 5,5'-diamide-2,2'-bipyridines and investigated their photochemical properties. In particular, these complexes were found to act as sensors for a variety of anions by strongly binding with them via cooperative hydrogen bonding between the amide hydrogen (NH) in three the ligands and anions.

Report

(4 results)
  • 2004 Annual Research Report   Final Research Report Summary
  • 2003 Annual Research Report
  • 2002 Annual Research Report
  • Research Products

    (13 results)

All 2005 2004 2003 2002 Other

All Journal Article (8 results) Patent(Industrial Property Rights) (3 results) Publications (2 results)

  • [Journal Article] Molecular Design of Peptides That Contain 5'-Amino-2,2'-Bipyridine-5-Carboxylic Acid As an Unnatural Amino Acid : Model Studies on Photo-Function And Stereochemistry of the Metal Complexes2005

    • Author(s)
      H.Ishida, M.Kyakuno, S.Minami, S.Oishi
    • Journal Title

      Peptides 2004 (in press)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      2004 Annual Research Report 2004 Final Research Report Summary
  • [Journal Article] Molecular Design of Peptides That Contain 5'-Amino-2,2'-Bipyridine-5-Carboxylic Acid As an Unnatural Amino Acid : Model Studies on Photo-Function And Stereochemistry of the Metal Complexes2005

    • Author(s)
      Hitoshi Ishida, Masato Kyakuno, Shintaro, Minami, Shigero Oishi
    • Journal Title

      Peptides 2004 (in press)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      2004 Final Research Report Summary
  • [Journal Article] Molecular Design of Functional Peptides by Utilizing Unnatural Amino Acids : Toward Artificial and Photo-functional Protein2004

    • Author(s)
      H.Ishida, M.Kyakuno, S.Oishi
    • Journal Title

      Biopolymers (Peptide Science) 76

      Pages: 69-82

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      2004 Annual Research Report 2004 Final Research Report Summary
  • [Journal Article] Molecular Design of Functional Peptides by Utilizing Unnatural Amino Acids That Can Coordinate with Metal Ions2004

    • Author(s)
      H.Ishida, M.Kyakuno, T.Nakazato, M.Fujii, S.Oishi
    • Journal Title

      Peptide Revolution : Genomics, Proteomics & Therapeutics

      Pages: 165-166

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      2004 Final Research Report Summary
  • [Journal Article] Molecular Design of Functional Peptides by Utilizing Unnatural Amino Acids : Toward Artificial and Photo-functional Protein2004

    • Author(s)
      Hitoshi Ishida, Masato Kyakuno, Shigero Oishi
    • Journal Title

      Biopolymers(Peptide Science) 76

      Pages: 69-82

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      2004 Final Research Report Summary
  • [Journal Article] Molecular Design of Functional Peptides by Utilizing Unnatural Amino Acids That Can Coordinate with Metal Ions2004

    • Author(s)
      Hitoshi Ishida, Masato Kyakuno, Takahiro Nakazato, Mina Fujii, Shigero Oishi
    • Journal Title

      Peptide Revolution : Genomics, Proteomics & Therapeutics(Eds.Michael Chorev and Tomi K.Sawyer)(American Peptide Society, U.S.A.)

      Pages: 165-166

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      2004 Final Research Report Summary
  • [Journal Article] Molecular Design of Functional Peptides by Utilizing Unnatural Amino Acids : Toward Artificial and Photo-functional Protein2003

    • Author(s)
      H.Ishida, M.Kyakuno, S.Oishi
    • Journal Title

      Biomolecular Chemistry - A Bridge for the Future -

      Pages: 172-175

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      2004 Final Research Report Summary
  • [Journal Article] Molecular Design of Functional Peptides by Utilizing Unnatural Amino Acids : Toward Artificial and Photo-functional Protein2003

    • Author(s)
      Hitoshi Ishida, Masato Kyakuno, Shigero Oishi
    • Journal Title

      Biomolecular Chemistry-A Bridge for the Future-(Eds.Yoshinobu Baba)(Maruzen, Tokyo, Japan)

      Pages: 172-175

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      2004 Final Research Report Summary
  • [Patent(Industrial Property Rights)] 有機発光性化合物2004

    • Inventor(s)
      石田 斉, 大石 茂郎
    • Industrial Property Rights Holder
      科学技術振興事業団
    • Industrial Property Number
      2004-100950
    • Filing Date
      2004-03-30
    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      2004 Final Research Report Summary
  • [Patent(Industrial Property Rights)] 有機発光性化合物2004

    • Inventor(s)
      石田 斉, 大石茂郎
    • Industrial Property Rights Holder
      科学技術振興事業団
    • Industrial Property Number
      2004-100950
    • Filing Date
      2004-03-30
    • Related Report
      2004 Annual Research Report
  • [Patent(Industrial Property Rights)] 高効率な有機発光性化合物2002

    • Inventor(s)
      石田 斉, 大石 茂郎
    • Industrial Property Rights Holder
      科学技術振興事業団
    • Industrial Property Number
      2002-237781
    • Filing Date
      2002-08-19
    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      2004 Final Research Report Summary
  • [Publications] H.Ishida, M.Kyakuno, S.Oishi: "Molecular Design of Functional Peptides by Utilizing Unnatural Amino Acids : Toward Artificial and Photo-functional Protein"Biopolymers (Peptide Science). 76(1). 69-82 (2004)

    • Related Report
      2003 Annual Research Report
  • [Publications] W.R.Brown, et al.: "Structural and Photophysical Characterisation of Coordination and Optical Isomers of Mononuclear Ruthenium(II) Polypyridyl 1,2,4-Triazole Complexes"Dalton Transactions. 2003. 2597-2602 (2003)

    • Related Report
      2003 Annual Research Report

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Published: 2002-04-01   Modified: 2016-04-21  

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