Michio Iwaoka

Summary

Affiliation: Tokai University
Country: Japan

Publications

  1. doi request reprint Mimicking the lipid peroxidation inhibitory activity of phospholipid hydroperoxide glutathione peroxidase (GPx4) by using fatty acid conjugates of a water-soluble selenolane
    Michio Iwaoka
    Department of Chemistry, School of Science, Tokai University, Kitakaname, Hiratsuka shi, Kanagawa 259 1292, Japan
    Molecules 20:12364-75. 2015
  2. doi request reprint Fatty acid conjugates of water-soluble (±)-trans-Selenolane-3,4-diol: effects of alkyl chain length on the antioxidant capacity
    Michio Iwaoka
    Department of Chemistry, School of Science, Tokai University, Kitakaname, Hiratsuka shi, Kanagawa 259 1292 Japan
    Chembiochem 16:1226-34. 2015
  3. pmc A water-soluble selenoxide reagent as a useful probe for the reactivity and folding of polythiol peptides
    Kenta Arai
    Department of Chemistry, School of Science, Tokai University, Kitakaname, Hiratsuka shi, Kanagawa 259 1292, Japan
    FEBS Open Bio 3:55-64. 2013
  4. pmc Reinvestigation of the oxidative folding pathways of hen egg white lysozyme: switching of the major pathways by temperature control
    Kenta Arai
    Department of Chemistry, School of Science, Tokai University, Kitakaname, Hiratsuka shi, Kanagawa 259 1292, Japan
    Int J Mol Sci 14:13194-212. 2013
  5. doi request reprint Hypervalent nonbonded interactions of a divalent sulfur atom. Implications in protein architecture and the functions
    Michio Iwaoka
    Department of Chemistry, School of Science, Tokai University, Kitakaname, Hiratsuka shi, Kanagawa 259 1292, Japan
    Molecules 17:7266-83. 2012
  6. doi request reprint The SAAP force field: development of the single amino acid potentials for 20 proteinogenic amino acids and Monte Carlo molecular simulation for short peptides
    Michio Iwaoka
    Department of Chemistry, School of Science, Tokai University, Kitakaname, Hiratsuka shi, Kanagawa 259 1292, Japan
    J Comput Chem 30:2039-55. 2009
  7. ncbi request reprint Importance of the single amino acid potential in water for secondary and tertiary structures of proteins
    Michio Iwaoka
    Department of Chemistry, School of Science, Tokai University, Kitakaname, Hiratsuka shi, Kanagawa 259 1292, Japan
    J Phys Chem B 110:14475-82. 2006
  8. doi request reprint Synthesis of selenocysteine and selenomethionine derivatives from sulfur-containing amino acids
    Michio Iwaoka
    Department of Chemistry, School of Science, Tokai University, Kitakaname, Hiratsuka shi, Kanagawa 259 1292, Japan
    Chem Biodivers 5:359-74. 2008
  9. doi request reprint Direct observation of conformational folding coupled with disulphide rearrangement by using a water-soluble selenoxide reagent--a case of oxidative regeneration of ribonuclease A under weakly basic conditions
    Michio Iwaoka
    Department of Chemistry, School of Science, Tokai University, Kitakaname, Hiratsuka shi, Kanagawa 259 1292, Japan
    J Biochem 144:121-30. 2008
  10. doi request reprint Rapid and quantitative disulfide bond formation for a polypeptide chain using a cyclic selenoxide reagent in an aqueous medium
    Kenta Arai
    Department of Chemistry, School of Science, Tokai University, Kitakaname, Hiratsuka shi, Kanagawa 259 1292, Japan
    Chemistry 17:481-5. 2011

Collaborators

  • Amit Kunwar
  • K Indira Priyadarsini
  • Naoki Kimura
  • Kenta Arai
  • Fumio Kumakura
  • Toshiki Takei
  • Kenichi Dedachi
  • Motoi Takahira
  • Toshiki Suzuki
  • Nozomi Kuroda
  • Natsumi Sekiyama
  • Akinobu Ogawa
  • Yoshiko Urabe
  • Takeshi Nomura
  • Kenji Moriai
  • Yuya Asahina
  • Hironobu Hojo
  • Wataru Shibagaki
  • Reina Shinozaki
  • Setsuko Ando
  • Kyoko Takayama
  • Yurika Kubo
  • Beena G Singh
  • Masato Noguchi
  • Katsuhiko Fujio

Detail Information

Publications17

  1. doi request reprint Mimicking the lipid peroxidation inhibitory activity of phospholipid hydroperoxide glutathione peroxidase (GPx4) by using fatty acid conjugates of a water-soluble selenolane
    Michio Iwaoka
    Department of Chemistry, School of Science, Tokai University, Kitakaname, Hiratsuka shi, Kanagawa 259 1292, Japan
    Molecules 20:12364-75. 2015
    ..Importance of the balance between hydrophilicity and lipophilicity for the design of effective GPx4 mimics was suggested. ..
  2. doi request reprint Fatty acid conjugates of water-soluble (±)-trans-Selenolane-3,4-diol: effects of alkyl chain length on the antioxidant capacity
    Michio Iwaoka
    Department of Chemistry, School of Science, Tokai University, Kitakaname, Hiratsuka shi, Kanagawa 259 1292 Japan
    Chembiochem 16:1226-34. 2015
    ..The activity can be controlled by the alkyl chain length...
  3. pmc A water-soluble selenoxide reagent as a useful probe for the reactivity and folding of polythiol peptides
    Kenta Arai
    Department of Chemistry, School of Science, Tokai University, Kitakaname, Hiratsuka shi, Kanagawa 259 1292, Japan
    FEBS Open Bio 3:55-64. 2013
    ..The stochastic behaviors as well as the absolute values of the second-order rate constants in comparison to dithiothreitol (DTT(red)) are useful to probe the chemical reactivity and conformation, hence the folding, of polypeptide chains...
  4. pmc Reinvestigation of the oxidative folding pathways of hen egg white lysozyme: switching of the major pathways by temperature control
    Kenta Arai
    Department of Chemistry, School of Science, Tokai University, Kitakaname, Hiratsuka shi, Kanagawa 259 1292, Japan
    Int J Mol Sci 14:13194-212. 2013
    ..At 35 °C, on the other hand, des[64-80] and des[6-127] were no longer stable, and only des[76-94] was populated. The results suggested that the major folding pathways of HEL can be switched from one to the other by temperature control. ..
  5. doi request reprint Hypervalent nonbonded interactions of a divalent sulfur atom. Implications in protein architecture and the functions
    Michio Iwaoka
    Department of Chemistry, School of Science, Tokai University, Kitakaname, Hiratsuka shi, Kanagawa 259 1292, Japan
    Molecules 17:7266-83. 2012
    ..Thus, S···X interactions will be useful tools for protein engineering and the ligand design...
  6. doi request reprint The SAAP force field: development of the single amino acid potentials for 20 proteinogenic amino acids and Monte Carlo molecular simulation for short peptides
    Michio Iwaoka
    Department of Chemistry, School of Science, Tokai University, Kitakaname, Hiratsuka shi, Kanagawa 259 1292, Japan
    J Comput Chem 30:2039-55. 2009
    ..It was suggested that the SAAP force field is a useful tool for analyzing conformations of polypeptides in terms of intrinsic conformational propensities of the single amino acid units...
  7. ncbi request reprint Importance of the single amino acid potential in water for secondary and tertiary structures of proteins
    Michio Iwaoka
    Department of Chemistry, School of Science, Tokai University, Kitakaname, Hiratsuka shi, Kanagawa 259 1292, Japan
    J Phys Chem B 110:14475-82. 2006
    ..e., the SAAPs) in water are of significant importance not only for describing conformations of a polypeptide chain in the random coil state but also for understanding the folding to the secondary and tertiary structures...
  8. doi request reprint Synthesis of selenocysteine and selenomethionine derivatives from sulfur-containing amino acids
    Michio Iwaoka
    Department of Chemistry, School of Science, Tokai University, Kitakaname, Hiratsuka shi, Kanagawa 259 1292, Japan
    Chem Biodivers 5:359-74. 2008
    ..The S-->Se modification (i.e., the chemical atomic mutation) would be a useful approach to peptide synthesis involving selenoamino acid residues...
  9. doi request reprint Direct observation of conformational folding coupled with disulphide rearrangement by using a water-soluble selenoxide reagent--a case of oxidative regeneration of ribonuclease A under weakly basic conditions
    Michio Iwaoka
    Department of Chemistry, School of Science, Tokai University, Kitakaname, Hiratsuka shi, Kanagawa 259 1292, Japan
    J Biochem 144:121-30. 2008
    ..Thus, DHS(ox) allowed facile identification of the conformational folding steps coupled with SS rearrangement on the major oxidative folding pathways...
  10. doi request reprint Rapid and quantitative disulfide bond formation for a polypeptide chain using a cyclic selenoxide reagent in an aqueous medium
    Kenta Arai
    Department of Chemistry, School of Science, Tokai University, Kitakaname, Hiratsuka shi, Kanagawa 259 1292, Japan
    Chemistry 17:481-5. 2011
    ..The results clearly demonstrated that the rate-determining step of the SS formation reaction is the first bimolecular process between a thiol substrate and DHS(ox) rather than the subsequent process to release a SS product...
  11. doi request reprint Characterization of kinetic and thermodynamic phases in the prefolding process of bovine pancreatic ribonuclease A coupled with fast SS formation and SS reshuffling
    Kenta Arai
    Department of Chemistry, School of Science, Tokai University, Kitakaname, Hiratsuka shi, Kanagawa 259 1292, Japan
    Biochemistry 49:10535-42. 2010
    ..The transition from kinetically formed to thermodynamically stabilized SS intermediates would be induced by hydrophobic nucleation as well as generation of the native interactions...
  12. doi request reprint Effects of ring size and polar functional groups on the glutathione peroxidase-like antioxidant activity of water-soluble cyclic selenides
    Kenta Arai
    Department of Chemistry, School of Science, Tokai University, Kitakaname, Hiratsuka shi, Kanagawa 259 1292, Japan
    J Org Chem 80:5633-42. 2015
    ..In methanol, however, the activity rank could not be explained by the simple scenarios applicable in water. ..
  13. doi request reprint Model study using designed selenopeptides on the importance of the catalytic triad for the antioxidative functions of glutathione peroxidase
    Toshiki Takei
    Department of Chemistry, School of Science, Tokai University, Kitakaname, Hiratsuka shi, Kanagawa 259 1292, Japan
    J Phys Chem B 118:492-500. 2014
    ..These experimental observations were supported by SAAP-MC simulation as well as by ab initio calculation. The latter further suggested that the interaction mode among the triad changes depending on the intermediate states. ..
  14. pmc Kinetic and thermodynamic analysis of the conformational folding process of SS-reduced bovine pancreatic ribonuclease A using a selenoxide reagent with high oxidizing ability
    Kenta Arai
    Department of Chemistry, School of Science, Tokai University, Kitakaname, Hiratsuka shi, Kanagawa 259 1292, Japan
    FEBS Open Bio 2:60-70. 2012
    ..It was revealed that DHS(ox) is useful for kinetic and thermodynamic analysis of the conformational folding process on the oxidative folding pathways of SS-reduced proteins...
  15. doi request reprint An amphiphilic selenide catalyst behaves like a hybrid mimic of protein disulfide isomerase and glutathione peroxidase 7
    Kenta Arai
    Department of Chemistry, School of Science, Tokai University, Kitakaname, Hiratsuka shi, Kanagawa 259 1292 Japan
    Chem Asian J 9:3464-71. 2014
    ..The combination of a water-soluble selenide and a long-chain alkyl group would be a useful motif in designing medicines for both protein misfolding diseases and antioxidant therapy...
  16. ncbi request reprint The SAAP force field. A simple approach to a new all-atom protein force field by using single amino acid potential (SAAP) functions in various solvents
    Michio Iwaoka
    Department of Life Sciences, Graduate School of Arts and Sciences, The University of Tokyo, Komaba, Meguro ku, Tokyo 153 8902, Japan
    J Comput Chem 24:1192-200. 2003
    ..e., the E(SAAP) term) may play definitive roles on the topologies of protein secondary structures...
  17. ncbi request reprint Statistical and theoretical investigations on the directionality of nonbonded S...O interactions. Implications for molecular design and protein engineering
    Michio Iwaoka
    Department of Life Sciences, Graduate School of Arts and Sciences, The University of Tokyo, Komaba, Meguro ku, Tokyo 153 8902, Japan
    J Am Chem Soc 124:10613-20. 2002
    ..The results suggested that S.O interactions may control protein structures to some extent and that the unique directional properties of S...O interactions could be applied to molecular design...