Ryuji Tanimura
Toray Industries
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Publication
Featured researches published by Ryuji Tanimura.
Nature Biotechnology | 1998
Ikuo Fujii; Shiro Fukuyama; Yoshiharu Iwabuchi; Ryuji Tanimura
In vitro affinity maturation for evolving catalytic antibodies has been demonstrated by generating a diverse repertoire of the appropriate complementarity-determining regions on a phage surface. Phage display is followed by a selection based on binding to an altered antigen that was not used at the time of immunization, and provides variants with new catalytic activity and substrate specificity. This library format reduces the time needed to isolate the desired catalytic antibody fragments to under 2 weeks.
FEBS Open Bio | 2015
Mikiya Satoh; Hajime Saburi; Tomoyuki U. Tanaka; Yoshinori Matsuura; Hisashi Naitow; Rieko Shimozono; Naoyoshi Yamamoto; Hideki Inoue; Noriko Nakamura; Yoshitaka Yoshizawa; Takumi Aoki; Ryuji Tanimura; Naoki Kunishima
Keap1 protein acts as a cellular sensor for oxidative stresses and regulates the transcription level of antioxidant genes through the ubiquitination of a corresponding transcription factor, Nrf2. A small molecule capable of binding to the Nrf2 interaction site of Keap1 could be a useful medicine. Here, we report two crystal structures, referred to as the soaking and the cocrystallization forms, of the Kelch domain of Keap1 with a small molecule, Ligand1. In these two forms, the Ligand1 molecule occupied the binding site of Keap1 so as to mimic the ETGE motif of Nrf2, although the mode of binding differed in the two forms. Because the Ligand1 molecule mediated the crystal packing in both the forms, the influence of crystal packing on the ligand binding was examined using a molecular dynamics (MD) simulation in aqueous conditions. In the MD structures from the soaking form, the ligand remained bound to Keap1 for over 20 ns, whereas the ligand tended to dissociate in the cocrystallization form. The MD structures could be classified into a few clusters that were related to but distinct from the crystal structures, indicating that the binding modes observed in crystals might be atypical of those in solution. However, the dominant ligand recognition residues in the crystal structures were commonly used in the MD structures to anchor the ligand. Therefore, the present structural information together with the MD simulation will be a useful basis for pharmaceutical drug development.
Journal of Biological Chemistry | 2009
Kozue Kato-Takagaki; Yumiko Mizukoshi; Yoshitaka Yoshizawa; Daisuke Akazawa; Yuichi Torii; Katsuki Ono; Ryuji Tanimura; Ichio Shimada; Hideo Takahashi
Glycoprotein VI (GPVI) is a major collagen receptor on the platelet surface that recognizes the glycine-proline-hydroxyproline (GPO) sequence in the collagen molecule and plays a crucial role in thrombus formation. Inhibitors that block the interaction of GPVI with collagen have potential for use as antithrombotic drugs. For low molecular weight drug design for GPVI, it is essential to obtain precise structural and interaction information about GPVI-binding ligands. However, experimentally obtained structural and interaction information of small ligands, such as peptides, in the GPVI-bound state has not been reported. In this study, by screening a phage-displayed peptide library, we discovered a novel peptide ligand (pep-10L; YSDTDWLYFSTS) without any similarities to the sequence of collagen that inhibits GPVI-GPO binding. Systematic Ala scanning in surface plasmon resonance experiments and a saturation transfer difference NMR experiment revealed that Trp6, Leu7, Phe9, and Ser10 residues in the pep-10L peptide interacted with GPVI. Furthermore, the GPVI-bound conformation of the pep-10L peptide was determined using transferred nuclear Overhauser effect analysis. The obtained structure has revealed that the central part of pep-10L (Asp5–Phe9) has a helical conformation, the side chains of Trp6, Leu7, and Phe9 form a hydrophobic side in the helix, and the Tyr8 side chain faces the opposite direction from the hydrophobic side. Computational docking prediction has shown that the hydrophobic side of pep-10L sticks in the hydrophobic groove on the GPVI surface, which corresponds to the putative collagen-related peptide binding groove. These data could enable the structure-guided development of a small molecule GPVI antagonist.
Bioorganic & Medicinal Chemistry Letters | 2017
Shinya Suzuki; Yuji Sugawara; Riichiro Tsuji; Ryuji Tanimura; Chihiro Kaneko; Natsumi Yuzawa; Mai Yagi; Koji Kawai
κ-Opioid receptor agonists with high selectivity over the μ-opioid receptor are attractive targets in the development of drugs for pain and pruritus. We previously reported the synthesis of 10α-hydroxy TRK-820 (1). In this study, we elucidated the biological properties of 1 and optimized its 6-acyl unit by modifying our synthetic route. Among the 10α-hydroxy TRK-820 derivatives prepared, 26 showed the most potent κ-opioid agonist activity (EC50=0.00466nM) and excellent selectivity and 22 was the most κ-selective agonist.
Chemical & Pharmaceutical Bulletin | 2017
Shinya Suzuki; Yuji Sugawara; Hideaki Inada; Riichiro Tsuji; Atsushi Inoue; Ryuji Tanimura; Rieko Shimozono; Mitsuhiro Konno; Tomofumi Ohyama; Eriko Higashi; Chizuka Sakai; Koji Kawai
κ-Opioid receptor agonists with high selectivity over the μ-opioid receptor and peripheral selectivity are attractive targets in the development of drugs for pain. We have previously attempted to create novel analgesics with peripheral selective κ-opioid receptor agonist on the basis of TRK-820. In this study, we elucidated the biological properties of 17-hydroxy-cyclopropylmethyl and 10α-hydroxy derivatives. These compounds were found to have better κ-opioid receptor selectivity and peripheral selectivity than TRK-820.
Journal of Biological Chemistry | 1996
Michiyuki Matsuda; Satoshi Ota; Ryuji Tanimura; Haruki Nakamura; Koozi Matuoka; Tadaomi Takenawa; Kazuo Nagashima; Takeshi Kurata
Protein Science | 1994
Ryuji Tanimura; Akinori Kidera; Haruki Nakamura
Journal of Molecular Biology | 1997
Hideaki Miyashita; Tomoko Hara; Ryuji Tanimura; Shiro Fukuyama; Christine Cagnon; Atsuko Kohara; Ikuo Fujii
Journal of Molecular Biology | 1997
Hideki Hatanaka; Ryuji Tanimura; Sakae Katoh; Fuyuhiko Inagaki
Journal of Medicinal Chemistry | 2010
Katsuki Ono; Hiroshi Ueda; Yoshitaka Yoshizawa; Daisuke Akazawa; Ryuji Tanimura; Ichio Shimada; Hideo Takahashi
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National Institute of Advanced Industrial Science and Technology
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