KATO Tamaki

写真a

Title

Associate Professor

Laboratory

2-4 Hibikino, Wakamatsu-ku, Kitakyushu-shi, Fukuoka

Research Fields, Keywords

Undergraduate Education 【 display / non-display

  • 1986.03   Kyushu University   Faculty of Science   Chemistry   Graduated   JAPAN

Post Graduate Education 【 display / non-display

  • 1991.03  Kyushu University  Graduate School, Division of Natural Science  Chemistry  Doctoral Program  Unfinished Course  JAPAN

Degree 【 display / non-display

  • Kyushu University -  Doctor of Science  1994.09

Biography in Kyutech 【 display / non-display

  • 2014.04
    -
    Now

    Kyushu Institute of TechnologyGraduate School of Life Science and Systems Engineering   Department of Biological Functions Engineering   Associate Professor  

Biography before Kyutech 【 display / non-display

  • 1991.04
    -
    1995.03

      Research Assistant   JAPAN

Specialized Field (scientific research fund) 【 display / non-display

  • Biomolecular chemistry

  • Biomolecular chemistry

 

Publications (Article) 【 display / non-display

  • Dual emissive bispyrene peptide probes for highly sensitive measurements of trypsin activity and evaluation of trypsin inhibitors

      26 ( 12 ) 3468 - 3473   2018.07  [Refereed]

     View Summary

    © 2018 Elsevier Ltd Peptide substrates were double labeled with pyrenes to prepare fluorescent probes for highly sensitive detection of protease activity and evaluation of protease inhibitors using pyrene monomer/excimer signals. Two proximate pyrene moieties formed excited state dimers in the probes, and these pyrene excimer formations were dissociated by tryptic digestion. The specificity constant of the optimum bispyrene peptide probe was 2.7 times higher than that of the conventional peptide-4-methylcoumarin amide. Moreover, our probe had high sensitivity with an estimated detection limit for trypsin of 4.11 pM. The half maximal inhibitory concentration and dissociation constant of the Bowman–Birk inhibitor were successfully estimated.

    DOI Scopus

  • Photophysical Characterization and BSA Interaction of Direct Ring Carboxy Functionalized Symmetrical squaraine Dyes

      924 ( 1 )   2017.12  [Refereed]

     View Summary

    © Published under licence by IOP Publishing Ltd. A series of far-red sensitive symmetrical squaraine dyes bearing direct-COOH functionalized indole ring were synthesized, characterized and subjected to photophysical investigations. These symmetrical squaraine dyes were then subjected to investigate their interaction with bovine serum albumin (BSA) in Phosphate buffer solutions. All the squaraine dyes under investigation exhibit intense and sharp optical absorption mainly in the far-red wavelength region from 550 nm-700 nm having very high molar extinction coefficients from 1.3 × 10 5 dm 3 .mol -1 .cm -1 . A very small Stokes shift of 10-17 nm indicates the rigid conformational structure of squaraine chromophore. Interaction of these dyes with BSA leads to not only enhanced emission intensity but also bathochromically shifted absorption maximum due to formation of dye-BSA conjugate. These dyes bind strongly with BSA having about an order of magnitude higher binding constant as compared to the reported squaraine dyes. Amongst the symmetrical squaraine dyes investigated in this work one bearing substituents like trifluorobutyl as alkyl chain at N-position of indole ring and carboxylic acid on benzene ring at the terminal (SQ-26) exhibited highest association with the BSA having very high binding constant 8.01 × 10 6 M -1 .

    DOI Scopus

  • Efficient near infrared fluorescence detection of elastase enzyme using peptide-bound unsymmetrical squaraine dye

      27   4024 - 4029   2017.06  [Refereed]

    DOI

  • Photophysical characterization and BSA interaction of the direct ring carboxy functionalized unsymmetrical NIR cyanine dyes

      140   6 - 13   2017.01  [Refereed]

    DOI

  • Novel fluorescent substrates for detection of trypsin activity and inhibitor screening by self-quenching

      26 ( 23 ) 5736 - 5740   2016.12  [Refereed]

     View Summary

    © 2016 Elsevier Ltd A group of self-quenching-based substrates with two fluorescent peptides for detection of trypsin activity was designed and synthesized. The substrates could be easily synthesized using simple solid-phase peptide synthesis techniques. Two fluorescent peptide substrates for trypsin were conjugated to the amino groups of lysine as a branched unit. The fluorescence of these substrates was self-quenched owing to the highly assembled fluorophores on the substrates. The release of these concentrated fluorophores by proteases allows for fluorescence recovery. Self-quenching reduced the fluorescence of the substrates by 64.1%, and the fluorescence intensity was recovered by the release of the fluorophores from the substrate peptides via tryptic cleavage. The kinetic assay revealed that the k cat /K m values of the substrates were almost comparable to those of the standard fluorescent probe, peptide-MCA. The detection limit for trypsin was 111 pM, and the calculation of IC 50 and K i values for the Bowman–Birk inhibitor was achieved using these substrates. These easily synthesizable self-quenching-based substrates have the potential to be useful for the detection of other disease-related protease activities.

    DOI Scopus

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Conference Prsentations (Oral, Poster) 【 display / non-display

  • 蛍光性ペプチドとリシンデンドリマーを用いた酵素活性の検出

    服部司 生命体工学研究科生体機能専攻

    日本化学会第91春季年会(2011)  (日本 横浜市)  2011.03  -  2011.03 

  • 固定化した蛍光性ペプチドによる酵素活性の検出

    山本祥太郎 物質工学科応用化学コース

    日本化学会第91春季年会(2011)  (日本 横浜市)  2011.03  -  2011.03 

  • 環状ペプチドナノチューブ形成の解析

    武哲 生命体工学研究科生体機能専攻

    日本化学会第91春季年会(2011)  (日本 横浜市)  2011.03  -  2011.03 

  • Synthesis and characterization of antimicrobial peptide surfactant with dendritic lysine groups

    5th International Peptide Symposium  2010.12  -  2010.12 

  • Cyclic Tetrapeptides containing iso-Propylglycine as Histone Deacetylase Inhibitors

    5th International Peptide Symposium  2010.12  -  2010.12 

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