Kyushu University Academic Staff Educational and Research Activities Database
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Takeru Nose Last modified date:2024.01.25



Graduate School
Undergraduate School
Other Organization
Administration Post
Vice President


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Homepage
https://kyushu-u.elsevierpure.com/en/persons/takeru-nose
 Reseacher Profiling Tool Kyushu University Pure
https://www.artsci.kyushu-u.ac.jp/~biomolchem/
Laboratory of Biomolecular Chemistry, Kyushu University .
Phone
092-802-6025
Fax
092-802-6025
Academic Degree
Ph. D
Country of degree conferring institution (Overseas)
No
Field of Specialization
Biochemistry
ORCID(Open Researcher and Contributor ID)
0000-0001-9771-7267
Total Priod of education and research career in the foreign country
00years03months
Outline Activities
○Management of KIKAN education
As the Vice President of Faculty of Arts and Science, I am in charge of organizing the overall KIKAN education.
As a member of the faculty, I manage the discipline subject (chemistry) and develops new subjects.
○Structure-activity relationship studies for receptor proteins and its ligands
○Development of a method for predicting the risk of environmental chemicals (environmental hormones).
○Bioactive peptide sciences, Elastin Peptides
Research
Research Interests
  • SAR studies for repetitive peptides
    keyword : peptide
    2013.04.
  • Total risk assessment system for endocrine disrupting chemicals
    keyword : endocrine disrupting chemistry, Nuclear receptor, computer modeling
    1998.04Total risk assessment of endocrine diruptor.
  • Structural and biological analysis for the activation mechanism of G-protein coupled receptor.
    keyword : G-protein coupled receptor
    1994.04Structure-function study of the activation mechanism of GPCR.
Academic Activities
Reports
1. High Efficiency Analytical Study on the Structure-activity Relationships of Peptidergic GPCR Ligands.
Papers
1. Keitaro Suyama, Masayuki Murashima, Iori Maeda, Takeru Nose, Enhancement of Aggregate Formation Through Aromatic Compound Adsorption in Elastin-like Peptide (FPGVG)5 Analogs., Biomacromolecules, 10.1021/acs.biomac.3c00779, 24, 11, 5265-5276, 2023.11, 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..
2. Shogo Sumiyoshi, Keitaro Suyama, Daiki Tatsubo, Naoki Tanaka, Keisuke Tomohara, Suguru Taniguchi, Iori Maeda, Takeru Nose, Metal ion scavenging activity of elastin-like peptide analogues containing a cadmium ion binding sequence, SCIENTIFIC REPORTS, 10.1038/s41598-022-05695-w, 12, 1, 2022.02, The development of simple and safe methods for recovering environmental pollutants, such as
heavy metals, is needed for sustainable environmental management. Short elastin‐like peptide (ELP) analogues conjugated with metal chelating agents are considered to be useful as metal sequestering agents as they are readily produced, environment friendly, and the metal binding domain can be selected based on any target metal of interest. Due to the temperature dependent self‐assembly
of ELP, the peptide‐based sequestering agents can be transformed from the solution state into
the particles that chelate metal ions, which can then be collected as precipitates. In this study, we developed a peptide‐based sequestering agent, AADAAC‐(FPGVG)4, by introducing the metal‐binding sequence AADAAC on the N‐terminus of a short ELP, (FPGVG)4. In turbidity measurements, AADAAC‐ (FPGVG)4 revealed strong self‐assembling ability in the presence of metal ions such as Cd2+ and Zn2+. The results from colorimetric analysis indicated that AADAAC‐(FPGVG)4 could capture Cd2+ and Zn2+. Furthermore, AADAAC‐(FPGVG)4 that bound to metal ions could be readily recycled by treatment with acidic solution without compromising its metal binding affinity. The present study indicates that the fusion of the metal‐binding sequence and ELP is a useful and powerful strategy to develop cost‐ effective heavy metal scavenging agents with low environmental impacts..
3. Keitaro Suyama, Shuhei Kaneko, Hitoshi Kesamaru, Xiaohui Liu, Ayami Matsushima, Yoshimitsu Kakuta, Takashi Okubo, Kazumi Kasatani, Takeru Nose, Evaluation of the Influence of Halogenation on the Binding of Bisphenol A to the Estrogen-Related Receptor γ, Chemical Research in Toxicology, 10.1021/acs.chemrestox.9b00379, 33, 4, 889-902, 2020.04, Halogenation of organic compounds is one the most important transformations in chemical synthesis and is used for the production of various industrial products. A variety of halogenated bisphenol analogs have recently been developed and are used as alternatives to bisphenol A (BPA), which is a raw material of polycarbonate that has adverse effects in animals. However, limited information is available on the potential toxicity of the halogenated BPA analogs. In the present study, to assess the latent toxicity of halogenated BPA analogs, we evaluated the binding and transcriptional activities of halogenated BPA analogs to the estrogen-related receptor γ(ERRγ), a nuclear receptor that contributes to the growth of nerves and sexual glands. Fluorinated BPA analogs demonstrated strong ERRγbinding potency, and inverse antagonistic activity, similar to BPA. X-ray crystallography and fragment molecular orbital (FMO) calculation revealed that a fluorine-substituted BPA analog could interact with several amino acid residues of ERRγ-LBD, strengthening the binding affinity of the analogs. The ERRγbinding affinity and transcriptional activity of the halogenated BPAs decreased with the increase in the size and number of halogen atom(s). The IC50 values, determined by the competitive binding assay, correlated well with the binding energy obtained from the docking calculation, suggesting that the docking calculation could correctly estimate the ERRγbinding potency of the BPA analogs. These results confirmed that ERRγhas a ligand binding pocket that fits very well to BPA. Furthermore, this study showed that the binding affinity of the BPA analogs can be predicted by the docking calculation, indicating the importance of the calculation method in the risk assessment of halogenated compounds..
4. Keitaro Suyama, Daiki Tatsubo, Wataru Iwasaki, Masaya Miyazaki, Yuhei Kiyota, Ichiro Takahashi, Iori Maeda, Takeru Nose, Enhancement of self-aggregation properties of linear elastin-derived short peptides by simple cyclization
strong self-aggregation properties of cyclo[FPGVG]n, consisting only of natural amino acids, Biomacromolecules, 10.1021/acs.biomac.8b00353, 19, 8, 3201-3211, 2018.06, Elastin-like peptides (ELP) consist of distinctive repetitive sequences, such as (VPGVG)n, exhibit temperature-dependent reversible self-assembly (coacervation), and have been considered to be useful for the development of thermo-responsive materials. Further fundamental studies evaluating coacervative properties of novel nonlinear ELPs could present design concepts for new thermo-responsive materials. In this study, we prepared novel ELPs, cyclic (FPGVG)n (cyclo[FPGVG]n, n = 1-5), and analyzed its self-assembly properties and structural characteristics. Cyclo[FPGVG]n (n = 3-5) demonstrated stronger coacervation capacity than the corresponding linear peptides. The coacervate of cyclo[FPGVG]5 was able to retain water-soluble dye molecules at 40°C, which implied that cyclo[FPGVG]5 could be employed as a base material of DDS (Drug Delivery System) matrices and other biomaterials. The results of molecular dynamics simulations and circular dichroism measurements suggested that a certain chain length was required for cyclo[FPGVG]n to demonstrate alterations in molecular structure that were critical to the exhibition of coacervation..
5. Daiki Tatsubo, Keitaro Suyama, Masaya Miyazaki, Iori Maeda, Takeru Nose, Stepwise Mechanism of Temperature-Dependent Coacervation of the Elastin-like Peptide Analogue Dimer, (C(WPGVG)3)2, Biochemistry, 10.1021/acs.biochem.7b01144, 57, 10, 1582-1590, 2018.02.
6. Keitaro Suyama, Suguru Taniguchi, Daiki Tatsubo, Iori Maeda, Takeru Nose, Dimerization effects on coacervation property of an elastin-derived synthetic peptide (FPGVG)5, Journal of Peptide Science, 10.1002/psc.2876, 22, 236-243, 2016.03.
7. Iori Maeda, Suguru Taniguchi, Noriko Watanabe, Asako Inoue, Yuko Yamazaki, Takeru Nose, Design of Phenylalanine-Containing Elastin-Derived Peptides Exhibiting Highly Potent Self-Assembling Capability , Protein & Peptide Letters, 10.2174/092986652210150821170703, 22, 10, 939-939, 2015.08, In this study, we developed a series of Phe-containing elastin-derived peptide-analogs, (Phe-Pro-Gly-Val-Gly)n (n = 1–5) and analyzed their reversible coacervation properties. Compared to the native elastin-derived repeating peptide sequence ((Val-Pro-Gly-Val-Gly)10), one of the Phecontaining 5-mer repeating peptide sequences ((Phe-Pro-Gly-Val-Gly)5) clearly exhibited stronger coacervation properties. The coacervation of (Phe-Pro-Gly-Val-Gly)5 is nearly the same as that of polypeptides (Val-Pro-Gly-Val-Gly)n (n > 40). Although large molecular weights (>10,000 Da) are generally required for the coacervation of elastin-derived peptides, (Phe-Pro-Gly-Val-Gly)5 exhibited reversible coacervation properties despite its low molecular weight (MW = 2,305 Da). High performance liquid chromatography (HPLC) and circular dichroism (CD) analysis revealed that (Phe-Pro-Gly-Val-Gly)5 has high hydrophobicity and an ordered structure with a type II β-turn, which contributes to the strong coacervation ability of the peptide. In addition, (Phe-Pro-Gly-Val-Gly)5 exhibited an effective particle size distribution (60–70 nm) at body temperature (37°C) and a dispersed small particle size similar to that of the monomer peptides at low temperatures. These properties, along with its small size and simple design, render the peptide suitable for use in biomaterials, including drug-delivery carriers..
8. Iori Maeda, Suguru Taniguchi, Junko Ebina, Noriko Watanabe, Takao Hattori, Takeru Nose, Comparison between Coacervation Property and Secondary Structure of Synthetic Peptides, Ile-containing Elastin-derived Pentapeptide Repeats, Protein and Peptide Letters, 10.2174/0929866511320080007, 20, 8, 905-910, 2013.08, A series of Ile-containing elastin-derived peptide-analogs, (Ile-Pro-Gly-Val-Gly)n (n=7–10) possessing remarkable and reversible coacervation property were newly synthesized. In comparison with the known elastin-derived peptideanalogs, which were so-called polypeptides, the obtained 35 to 50 mer peptides, (IPGVG)n (n=7–10) were significantly low molecular sized-polypeptides. However, they clearly exhibited coacervation property as same as the polypeptides did. Because of their low molecular size, spectrographic analyses of (IPGVG)n (n=7–10) became feasible to carry out. As results of secondary structural analyses by CD and FT-IR, it was found that the coacervation property of the peptides is clearly attributed to the ordered secondary-structures, mainly, type II β–turn..
9. Mitsuhiro Nishigori, Takeru Nose, Yasuyuki Shimohigashi, Highly Potent Binding and Inverse Agonist Activity of Bisphenol A Derivatives for Retinoid-related Orphan Nuclear Receptor RORg, Toxicol. Lett.,, 212, 2, 205-211, 2012.05.
10. Nose T., Tokunaga T., and Shimohigashi Y., Exploration of endocrine-disrupting chemicals on estrogen receptor α by the agonist/antagonist differential-docking screening (AADS) method: 4-(1-Adamantyl)phenol as a potent endocrine disruptor candidate, Toxicol. Lett.,, in press, 2009.11.
Membership in Academic Society
  • American Chemical Society
Educational
Educational Activities
I am engaged in the education of the research guidance concerning the structure-function biochemistry for the graduate of the doctor course, master course and bachelor course. I am also taking charge of the lecture of the biochemistry and the practice of the biochemistry experiment as an education of the undergraduate students.
Teaching classes:
1)KIKAN Education;
Kikan-Education Seminar, Interdisciplinary Collaborative Learning of Social Issues B, Elementary Inorganic Chemistry
2) Undergraduate School Education;
Biological chemistry III, Biochemistry Experiment (Bachelor Course of Department of Chemistry)
3) Graduate School Education;
Biochemistry lecture III (Masters Course of Department of Chemistry)
4) Education Innovation Initiative;
Responsible for reforming the teaching assistant (TA) system.

Other Educational Activities
  • 2023.01.
  • 2022.08.