Tokushima University / Educator and Researcher Directory --- Denda, Masaya

Personal Web Page

https://researchmap.jp/7000020585 (researchmap)

https://orcid.org/0000-0001-6820-2328 (ORCID)

Field of Study

○	Life sciences [Clinical pharmacy]
○	Life sciences [Pharmaceuticals - chemistry and drug development]

Subject of Study

Book / Paper

Book:

1.	Masaya Denda : 第9章チーム医療, Oct. 2020. (Keyword) 医療薬学 / 臨床薬学

Academic Paper (Judged Full Paper):

1.	Tsuji Takashi, Hayato INAZUKI, Kobayashi Daishiro, Hayashi JUNYA, Masaya Denda and Akira Otaka : Cysteinylprolyl ester-mediated drug release from a lipid-drug conjugate, Bioorganic & Medicinal Chemistry Letters, Vol.109, 129850, 2024. (Summary) For small-molecule drugs, lipidation via a cleavable linkage can extend half-life in circulation through interaction with albumin. Here we modified the cysteinylprolyl ester (CPE) system used in peptide thioester synthesis, which normally requires basic conditions, for use as an self-immolative linker and release device for a lipid-gemcitabine conjugate. To improve release under physiological conditions for medical application, a methyl group at the α-position of cysteine on the CPE unit was incorporated in anticipation of the Thorpe-Ingold effect. As a result, Ac-Gly-(α-Me)Cys(SH)-Pro-gemcitabine 11 drastically promoted the release of gemcitabine in comparison with Ac-Gly-Cys(SH)-Pro-gemcitabine 10. Furthermore, in the presence of bovine serum albumin and/or 2-mercaptoethanesulfonic acid, the gentle and continuous release of gemcitabine from the lipid-gemcitabine conjugate 16 was achieved. In addition to gemcitabine, this method could allow high clearance drugs, including nucleic acid and prostacyclin derivatives, to maintain their biological activity long enough to become effective. (Keyword) Gemcitabine / Deoxycytidine / Lipids / Esters / Drug Liberation / Cysteine / Humans / Molecular Structure / Serum Albumin, Bovine / Animals (Tokushima University Institutional Repository) ● Metadata: 119452 (Link to Publication Site) ● Publication site (DOI): 10.1016/j.bmcl.2024.129850 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 38879090 ● Summary page in Scopus @ Elsevier: 2-s2.0-85196376333 (Tokushima University Institutional Repository: 119452, DOI: 10.1016/j.bmcl.2024.129850, PubMed: 38879090, Elsevier: Scopus)
2.	Daishiro Kobayashi, Masaya Denda, Junya Hayashi, Kohta Hidaka, Yutaka Kohmura, Takaaki Tsunematsu, Kohei Nishino, Harunori Yoshikawa, OHKAWACHI Kento, Kiyomi Nigorikawa, Tetsuro Yoshimaru, Naozumi Ishimaru, Wataru Nomura, Toyomasa Katagiri, Hidetaka Kosako and Akira Otaka : Sulfoxide-Mediated Cys-Trp-Selective Bioconjugation that Enables Protein Labeling and Peptide Heterodimerization, ChemistryEurope, Vol.2, No.3-4, 2024. (Link to Publication Site) ● Publication site (DOI): 10.1002/ceur.202400014 (Link to Search Site for Scientific Articles) ● Search Scopus @ Elsevier (DOI): 10.1002/ceur.202400014 (DOI: 10.1002/ceur.202400014)
3.	Junya Hayashi, Daishiro Kobayashi, Masaya Denda and Akira Otaka : Late-stage formation of a sactionine linkage enabled by Lossen rearrangement of glycyl hydroxamic acid, Organic Letters, Vol.26, No.24, 5167-5171, 2024. (Summary) Late-stage formation of a sactionine thioether bond connecting a Gly α-carbon and Cys thiol was achieved by Lossen rearrangement of a glycyl hydroxamic acid (GlyHA) residue in a peptide. Lossen rearrangement allowed conversion of GlyHA within a peptide to an -acyl iminium equivalent, which subsequently reacted with -acetamidomethyl Cys (Cys(Acm)) in TFA in the presence of guanidine hydrochloride (Gn·HCl) to yield the desired thioether linkage in the final stage. (Tokushima University Institutional Repository) ● Metadata: 119421 (Link to Publication Site) ● Publication site (DOI): 10.1021/acs.orglett.4c01685 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 38848136 ● Summary page in Scopus @ Elsevier: 2-s2.0-85195570491 (Tokushima University Institutional Repository: 119421, DOI: 10.1021/acs.orglett.4c01685, PubMed: 38848136, Elsevier: Scopus)
4.	Junya Hayashi, Daishiro Kobayashi, Chizuru Namikawa, Masaya Denda and Akira Otaka : Synthesis of N-Glyoxylyl Peptides Enabled by a Lossen Rearrangement-Induced Intramolecular Redox Reaction of N-Terminal Glycyl Hydroxamic Acid, Organic Letters, Vol.26, No.20, 4246-4250, 2024. (Summary) An oxidant-free approach to the synthesis of -glyoxylyl peptides has been developed that utilizes the Lossen rearrangement of the N-terminal glycyl hydroxamic acid residue. The synthesis proceeds via an intramolecular redox mechanism to yield the glyoxylyl peptides, which are then subjected to various peptide cyclization procedures. The reaction scheme is suitable for oxidation-sensitive moieties including amino acids. (Tokushima University Institutional Repository) ● Metadata: 119346 (Link to Publication Site) ● Publication site (DOI): 10.1021/acs.orglett.4c01126 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 38738629 ● Search Scopus @ Elsevier (PMID): 38738629 ● Search Scopus @ Elsevier (DOI): 10.1021/acs.orglett.4c01126 (Tokushima University Institutional Repository: 119346, DOI: 10.1021/acs.orglett.4c01126, PubMed: 38738629)
5.	Kohta Hidaka, Daishiro Kobayashi, Junya Hayashi, Masaya Denda and Akira Otaka : Advanced Insulin Synthesis by One-pot/Stepwise Disulfide Bond Formation Enabled by S-Protected Cysteine Sulfoxide, Chemistry - A European Journal, Vol.30, No.39, e202401003, 2024. (Summary) An advanced insulin synthesis is presented that utilizes one-pot/stepwise disulfide bond formation enabled by acid-activated S-protected cysteine sulfoxides in the presence of chloride anion. S-chlorocysteine generated from cysteine sulfoxides reacts with an S-protected cysteine to afford S-sulfenylsulfonium cation, which then furnishes the disulfide or reversely returns to the starting materials depending on the S-protection employed and the reaction conditions. Use of S-acetamidomethyl cysteine (Cys(Acm)) and its sulfoxide (Cys(Acm)(O)) selectively give the disulfide under weak acid conditions in the presence of MgCl2 even if S-p-methoxybenzyl cysteine (Cys(MBzl)) and its sulfoxide (Cys(MBzl)(O)) are also present. In contrast, the S-MBzl pair yields the disulfide under more acidic conditions in the presence of a chloride anion source. These reaction conditions allowed a one-pot insulin synthesis. Additionally, lipidated insulin was prepared by a one-pot disulfide-bonding/lipidation sequence. (Tokushima University Institutional Repository) ● Metadata: 119333 (Link to Publication Site) ● Publication site (DOI): 10.1002/chem.202401003 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 38683139 ● Search Scopus @ Elsevier (PMID): 38683139 ● Search Scopus @ Elsevier (DOI): 10.1002/chem.202401003 (Tokushima University Institutional Repository: 119333, DOI: 10.1002/chem.202401003, PubMed: 38683139)
6.	Rin Miyajima, Kosuke Tanegashima, Naoto Naruse, Masaya Denda, Takahiro Hara and Akira Otaka : Identification of Low-Density Lipoprotein Receptor-Related Protein 1 as a CXCL14 Receptor Using Chemically Synthesized Tetrafunctional Probes, ACS Chemical Biology, Vol.19, No.2, 551-562, 2024. (Summary) CXCL14 is a primordial CXC-type chemokine that transports CpG oligodeoxynucleotides (ODN) into endosomes and lysosomes in dendritic cells, thereby leading to the activation of the Toll-like receptor 9 (TLR9)-mediated innate immune system. However, the underlying molecular mechanism by which the CXCL14-CpG ODN complex enters cells remains elusive. Herein, we describe the chemical synthesis of CXCL14-derived photoaffinity probes and their application to the identification of target receptors for CXCL14 using quantitative proteomics. By utilizing native chemical ligation and maleimide-thiol coupling chemistry, we synthesized site-specifically modified CXCL14-based photoaffinity probes that contain photoreactive 2-aryl-5-carboxytetrazole (ACT) and a hydrazine-labile cleavable linker. CXCL14-based probes were found to be capable of binding CpG ODN to immune cells, whose bioactivities were comparable to native CXCL14. Application of CXCL14-derived probes to quantitative proteomic experiments enabled the identification of dozens of target receptor candidates for CXCL14 in mouse macrophage-derived RAW264.7 cells, and we discovered that low-density lipoprotein receptor-related protein 1 (LRP1) is a novel receptor for CXCL14 by competitive proteome profiling. We further showed that disruption of LRP1 affected the incorporation of the CXCL14-CpG ODN complex in the cells. Overall, this report highlights the power of synthetic CXCL14-derived photoaffinity probes combined with chemical proteomics to discover previously unidentified receptors for CXCL14, which could promote an understanding of the molecular functions of CXCL14 and the elaborate machinery of innate immune systems. (Keyword) Animals / Mice / Low Density Lipoprotein Receptor-Related Protein-1 / Proteomics / Oligodeoxyribonucleotides / Lipoproteins, LDL / Chemokines, CXC (Link to Publication Site) ● Publication site (DOI): 10.1021/acschembio.3c00717 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 38289037 ● Search Scopus @ Elsevier (PMID): 38289037 ● Search Scopus @ Elsevier (DOI): 10.1021/acschembio.3c00717 (DOI: 10.1021/acschembio.3c00717, PubMed: 38289037)
7.	Masaki Imanishi, Takahisa Inoue, Keijo Fukushima, Ryosuke Yamashita, Ryo Nakayama, Masataka Nojima, Kosuke Kondo, Yoshiki Gomi, Honoka Tsunematsu, Kohei Goto, Licht Miyamoto, Masafumi Funamoto, Masaya Denda, Keisuke Ishizawa, Akira Otaka, Hiromichi Fujino, Yasumasa Ikeda and Koichiro Tsuchiya : CA9 and PRELID2; hypoxia-responsive potential therapeutic targets for pancreatic ductal adenocarcinoma as per bioinformatics analyses., Journal of Pharmacological Sciences, Vol.153, No.4, 232-242, 2023. (Summary) A strong hypoxic environment has been observed in pancreatic ductal adenocarcinoma (PDAC) cells, which contributes to drug resistance, tumor progression, and metastasis. Therefore, we performed bioinformatics analyses to investigate potential targets for the treatment of PDAC. To identify potential genes as effective PDAC treatment targets, we selected all genes whose expression level was related to worse overall survival (OS) in The Cancer Genome Atlas (TCGA) database and selected only the genes that matched with the genes upregulated due to hypoxia in pancreatic cancer cells in the dataset obtained from the Gene Expression Omnibus (GEO) database. Although the extracted 107 hypoxia-responsive genes included the genes that were slightly enriched in angiogenic factors, TCGA data analysis revealed that the expression level of endothelial cell (EC) markers did not affect OS. Finally, we selected CA9 and PRELID2 as potential targets for PDAC treatment and elucidated that a CA9 inhibitor, U-104, suppressed pancreatic cancer cell growth more effectively than 5-fluorouracil (5-FU) and PRELID2 siRNA treatment suppressed the cell growth stronger than CA9 siRNA treatment. Thus, we elucidated that specific inhibition of PRELID2 as well as CA9, extracted via exhaustive bioinformatic analyses of clinical datasets, could be a more effective strategy for PDAC treatment. (Keyword) Humans / Carbonic Anhydrase IX / Antigens, Neoplasm / Carcinoma, Pancreatic Ductal / Pancreatic Neoplasms / Hypoxia / RNA, Small Interfering / Computational Biology / Pancreatic Neoplasms (Tokushima University Institutional Repository) ● Metadata: 119176 (Link to Publication Site) ● Publication site (DOI): 10.1016/j.jphs.2023.10.003 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 37973221 ● CiNii @ National Institute of Informatics (CRID): 1872553967456110848 ● Search Scopus @ Elsevier (PMID): 37973221 ● Search Scopus @ Elsevier (DOI): 10.1016/j.jphs.2023.10.003 (Tokushima University Institutional Repository: 119176, DOI: 10.1016/j.jphs.2023.10.003, PubMed: 37973221, CiNii: 1872553967456110848)
8.	Takashi Tsuji, Honoka Tsunematsu, Masaki Imanishi, Masaya Denda, Koichiro Tsuchiya and Akira Otaka : Enhanced tumor specific drug release by hypoxia sensitive dual-prodrugs based on 2-nitroimidazole, Bioorganic & Medicinal Chemistry Letters, 129484, 2023. (Summary) Hypoxia in cancer is important in the development of cancer-selective medicines. Here, a novel hypoxia-responsible dual-prodrug is described. We designed and synthesized 2-nitroimidazole derivatives which spontaneously release both a PYG inhibitor and gemcitabine under hypoxic conditions. One such derivative, a prodrug 9 was found to be stable against chemical and enzymatic hydrolysis, and upon chemical reduction of the nitro group on imidazole, successfully releases both drugs. In an in vitro proliferation assay using human pancreatic cells, compound 9 exhibited significant anti-proliferative effects in hypoxia but fewer effects in normoxia. Consequently, prodrug 9 should be useful for cancer treatment due to its improved cancer selectivity and potential to overcome drug resistance. (Link to Publication Site) ● Publication site (DOI): 10.1016/j.bmcl.2023.129484 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 37716415 ● Search Scopus @ Elsevier (PMID): 37716415 ● Search Scopus @ Elsevier (DOI): 10.1016/j.bmcl.2023.129484 (DOI: 10.1016/j.bmcl.2023.129484, PubMed: 37716415)
9.	Mami Neishi, Hirofumi Hamano, Takahiro Niimura, Masaya Denda, Kenta Yagi, Koji Miyata, Tsung-Jen Lin, Tsukasa Higashionna, Mitsuhiro Goda, Yoshito Zamami, Keisuke Ishizawa and Hideki Nawa : Structural characterization of the optical isomers esomeprazole and omeprazole using the JADER and FAERS databases, Toxicology and Applied Pharmacology, Vol.475, 116632, 2023. (Summary) It is unclear whether the s (-) form of esomeprazole (EPZ) has an improved safety profile when compared with its racemic form omeprazole (OPZ). We assessed the potential complications of these optical isomers when combined with cilostazol, clopidogrel, and prasugrel, which are frequently used concomitant medications. Using two adverse event spontaneous reporting databases, Japanese Adverse Drug Event Report (JADER) and FDA Adverse Event Reporting System (FAERS), adverse event names for hemorrhage, venous/arterial embolization, and thrombus were obtained from the Medical Dictionary for Regulatory Activities. Reported odds ratios were calculated using a 2 × 2 contingency table, and a signal was considered present if the lower limit of the 95% confidence interval was >1. In combination with cilostazol, a hemorrhagic signal for OPZ in JADER and arterial emboli and thrombus signals for EPZ were detected in both databases. In combination with clopidogrel, OPZ showed arterial emboli and thrombus signals in JADER and venous/arterial emboli and thrombus signals in FAERS, while EPZ displayed arterial emboli and thrombus signals in FAERS. In contrast, when in combination with prasugrel, there were no adverse event signals in either database. This study has confirmed using big data, that EPZ, the optical isomer and racemic form of omeprazole, has the beneficial characteristics of being less sensitive to CYP, as was intended by its design. (Keyword) Humans / United States / Esomeprazole / Omeprazole / Clopidogrel / Prasugrel Hydrochloride / Cilostazol / Adverse Drug Reaction Reporting Systems / Hemorrhage / Drug-Related Side Effects and Adverse Reactions / Databases, Factual (Link to Publication Site) ● Publication site (DOI): 10.1016/j.taap.2023.116632 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 37482254 ● Summary page in Scopus @ Elsevier: 2-s2.0-85165980754 (DOI: 10.1016/j.taap.2023.116632, PubMed: 37482254, Elsevier: Scopus)
10.	OHKAWACHI Kento, Kaito Anzaki, Daishiro Kobayashi, Ryuji Kyan, Takuma Yasuda, Masaya Denda, Norio Harada, Akira Shigenaga, Nobuya Inagaki and Akira Otaka : Residue-selective CH sulfenylation enabled by acid-activated S-acetamidomethyl cysteine sulfoxide with application to one-pot stapling and lipidation sequence, Chemistry - A European Journal, Vol.29, No.26, e202300799, 2023. (Summary) A tyrosine (Tyr)- or tryptophan (Trp)-selective metal-free C-H sulfenylation reaction using an acid-activated S-acetamidomethyl cysteine (Cys) sulfoxide, Cys(Acm)(O), has been achieved. The dually protonated intermediate produced from Cys(Acm)(O) under acidic conditions allows the sulfenylation of Tyr. Significantly, the reaction in the presence of trimethylsilyl trifluoromethanesulfonate (TMSOTf) mainly affords a Cys-Tyr-linked peptide even in the presence of Trp residues. In contrast, a Cys-Trp-linked peptide was selectively obtained from the reaction in the presence of guanidine hydrochloride (Gn ⋅ HCl) under acidic conditions. Established Tyr- and Trp-selective sulfenylation methods were used in the Cys-Tyr stapling and Trp lipidation of glucagon-like peptides 1 in a one-pot/stepwise manner. Investigation of the mechanism showed that orbital- and charge-controlled reactions are responsible for the Trp and Tyr selectivity, respectively. (Keyword) Cysteine / Peptides / Tyrosine / Sulfoxides / Guanidine (Tokushima University Institutional Repository) ● Metadata: 118080 (Link to Publication Site) ● Publication site (DOI): 10.1002/chem.202300799 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 36922350 ● CiNii @ National Institute of Informatics (CRID): 1360861705587936000 ● Search Scopus @ Elsevier (PMID): 36922350 ● Search Scopus @ Elsevier (DOI): 10.1002/chem.202300799 (Tokushima University Institutional Repository: 118080, DOI: 10.1002/chem.202300799, PubMed: 36922350, CiNii: 1360861705587936000)
11.	Daishiroh Kobayashi, KURAOKA Eisuke, Junya Hayashi, Takuma Yasuda, Yutaka Kohmura, Masaya Denda, Norio Harada, Nobuya Inagaki and Akira Otaka : S-Protected cysteine sulfoxide-enabled tryptophan-selective modification with application to peptide lipidation, ACS Medicinal Chemistry Letters, Vol.13, No.7, 1125-1130, 2022. (Tokushima University Institutional Repository) ● Metadata: 117175 (Link to Publication Site) ● Publication site (DOI): 10.1021/acsmedchemlett.2c00161 (Link to Search Site for Scientific Articles) ● Search Scopus @ Elsevier (DOI): 10.1021/acsmedchemlett.2c00161 (Tokushima University Institutional Repository: 117175, DOI: 10.1021/acsmedchemlett.2c00161)
12.	Masato Miyake, Mitsuaki Sobajima, Kiyoe Kurahashi, Akira Shigenaga, Masaya Denda, Akira Otaka, Tomohide Saio, Naoki Sakane, Hidetaka Kosako and Seiichi Oyadomari : Identification of an endoplasmic reticulum proteostasis modulator that enhances insulin production in pancreatic β cells., Cell Chemical Biology, Vol.29, No.6, 996-1009.e9, 2022. (Summary) Perturbation of endoplasmic reticulum (ER) proteostasis is associated with impairment of cellular function in diverse diseases, especially the function of pancreatic β cells in type 2 diabetes. Restoration of ER proteostasis by small molecules shows therapeutic promise for type 2 diabetes. Here, using cell-based screening, we report identification of a chemical chaperone-like small molecule, KM04794, that alleviates ER stress. KM04794 prevented protein aggregation and cell death caused by ER stressors and a mutant insulin protein. We also found that this compound increased intracellular and secreted insulin levels in pancreatic β cells. Chemical biology and biochemical approaches revealed that the compound accumulated in the ER and interacted directly with the ER molecular chaperone BiP. Our data show that this corrector of ER proteostasis can enhance insulin storage and pancreatic β cell function. (Keyword) Diabetes Mellitus, Type 2 / Endoplasmic Reticulum / Endoplasmic Reticulum Stress / Humans / Insulin / Insulin-Secreting Cells / Proteostasis / Unfolded Protein Response (Tokushima University Institutional Repository) ● Metadata: 116761 (Link to Publication Site) ● Publication site (DOI): 10.1016/j.chembiol.2022.01.002 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 35143772 ● Search Scopus @ Elsevier (PMID): 35143772 ● Search Scopus @ Elsevier (DOI): 10.1016/j.chembiol.2022.01.002 (Tokushima University Institutional Repository: 116761, DOI: 10.1016/j.chembiol.2022.01.002, PubMed: 35143772)
13.	Daiki Sato, Masaya Denda, Honoka Tsunematsu, Naonobu Tanaka, Isamu Konishi, Chiaki Komiya, Akira Shigenaga and Akira Otaka : Late-stage macrolactonisation enabled by tandem acyl transfers followed by desulphurisation, Chemical Communications, Vol.58, No.17, 2918-2921, 2022. (Summary) Intramolecular -acylation of a thiol-installed threonine with a thioester unit, followed by S-O acyl transfer and subsequent desulphurisation, allows the synthesis of lactone peptides. A protocol has been developed enabling the cyclisation of a linear peptide, a reaction which has not been achieved by conventional methods. (Keyword) Lactones / Molecular Structure / Peptides / Sulfhydryl Compounds / Threonine (Tokushima University Institutional Repository) ● Metadata: 116717 (Link to Publication Site) ● Publication site (DOI): 10.1039/D1CC07248J (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 35138311 ● Search Scopus @ Elsevier (PMID): 35138311 ● Search Scopus @ Elsevier (DOI): 10.1039/D1CC07248J (Tokushima University Institutional Repository: 116717, DOI: 10.1039/D1CC07248J, PubMed: 35138311)
14.	Kazuto Nakae, Sho Masui, Atsushi Yonezawa, Motomu Hashimoto, Ryu Watanabe, Koichi Murata, Kosaku Murakami, Masao Tanaka, Hiromu Ito, Kotoko Yokoyama, Noriko Iwamoto, Takashi Shimada, Miyuki Nakamura, Masaya Denda, Kotaro Itohara, Shunsaku Nakagawa, Yasuaki Ikemi, Satoshi Imai, Takayuki Nakagawa, Makoto Hayakari and Kazuo Matsubara : Potential Application of Measuring Serum Infliximab Levels in Rheumatoid Arthritis Management: A Retrospective Study based on KURAMA Cohort Data, PLoS ONE, Vol.16, No.10, e0258601, 2021. (Summary) Infliximab (IFX) therapy has considerably improved the treatment of rheumatoid arthritis (RA). However, some patients still do not respond adequately to IFX therapy, or the efficacy of the treatment diminishes over time. Although previous studies have reported a relationship between serum IFX levels and therapeutic efficacy, the potential applications of IFX therapeutic drug monitoring (TDM) in clinical practice remain unclear. The purpose of this study was to investigate the potential applications of IFX TDM by analyzing a Japanese cohort database. Data were collected retrospectively from the Kyoto University Rheumatoid Arthritis Management Alliance cohort between January 1, 2011, and December 31, 2018. Serum IFX levels were measured using a liquid chromatography-tandem mass spectrometer. Out of the 311 RA patients that used IFX, 41 were eligible for the analysis. Serum IFX levels were significantly higher in responders than in non-responders. An optimal cut-off value was determined to be 0.32 μg/mL based on a receiver operating characteristic curve. At the IFX measurement point, a better therapeutic response was observed in the high IFX group (n = 32) than in the low IFX group (n = 9). Conversely, at the maximum effect point, when DAS28-ESR was the lowest between IFX introduction and measurement points, there were no differences in responder proportions between the low and high IFX groups. IFX primary ineffectiveness could be avoided with appropriate dose escalation without blood concentration measurement in clinical practice. In conclusion, IFX TDM could facilitate the identification of secondary non-responders and in turn, proper IFX use. (Keyword) Infliximab / Rheumatoid Arthritis / KURAMA Cohort (Link to Publication Site) ● Publication site (DOI): 10.1371/journal.pone.0258601 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 34644354 ● Search Scopus @ Elsevier (PMID): 34644354 ● Search Scopus @ Elsevier (DOI): 10.1371/journal.pone.0258601 (DOI: 10.1371/journal.pone.0258601, PubMed: 34644354)
15.	Daishiroh Kobayashi, Yutaka Kohmura, Junya Hayashi, Masaya Denda, Koichiro Tsuchiya and Akira Otaka : Copper (II)-mediated C-H sulphenylation or selenylation of tryptophan enabling macrocyclization of peptides, Chemical Communications, Vol.57, 10763-10766, 2021. (Tokushima University Institutional Repository) ● Metadata: 116325 (Link to Publication Site) ● Publication site (DOI): 10.1039/D1CC04856B (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 34585682 ● Search Scopus @ Elsevier (PMID): 34585682 ● Search Scopus @ Elsevier (DOI): 10.1039/D1CC04856B (Tokushima University Institutional Repository: 116325, DOI: 10.1039/D1CC04856B, PubMed: 34585682)
16.	Daishiroh Kobayashi, Yutaka Kohmura, Toshihiko Sugiki, Eisuke Kuraoka, Masaya Denda, Toshimichi Fujiwara and Akira Otaka : Peptide Cyclization Mediated by Metal-Free S-Arylation: S-Protected Cysteine Sulfoxide as an Umpolung of Cysteine Nucleophile, Chemistry - A European Journal, Vol.27, No.56, 14092-14099, 2021. (Tokushima University Institutional Repository) ● Metadata: 116324 (Link to Publication Site) ● Publication site (DOI): 10.1002/chem.202102420 (Link to Search Site for Scientific Articles) ● Search Scopus @ Elsevier (DOI): 10.1002/chem.202102420 (Tokushima University Institutional Repository: 116324, DOI: 10.1002/chem.202102420)
17.	Masahiro Ueda, Chiaki Komiya, Sayuki Arii, Kohshi Kusumoto, Masaya Denda, Keiichiro Okuhira, Akira Shigenaga and Akira Otaka : Sequence-independent traceless method for preparation of peptide/protein thioesters using CPaseY-mediated hydrazinolysis, Chemical & Pharmaceutical Bulletin, Vol.68, No.12, 1226-1232, 2020. (Summary) Proteins incorporating artificial moieties such as fluorophores and drugs have enjoyed increasing use in chemical biology and drug development research. Preparation of such artificial protein derivatives has relied mainly on native chemical ligation in which peptide/protein thioesters chemoselectively react with N-terminal cysteine peptides to afford protein molecules. The protein thioesters derived from expressed proteins represent thioesters that are very useful for the preparation of artificial proteins by native chemical ligation with synthetic peptides with N-terminal Cys. We recently have developed a traceless thioester-producing protocol using carboxypeptidase Y (CPaseY) which is compatible with an expressed protein. The traceless character is ensured by CPaseY-mediated hydrazinolysis of C-terminal Xaa (X)-Cys-Pro-Leu-OH sequence followed by an auto-processing of the Cys-Pro (CP) dipeptide unit, affording the corresponding X-thioester (X-SR). However, hydrazinolysis of the amide bond in the prolyl leucine junction depends significantly on the nature of X. In the case of hydrophobic X residues, the hydrazinolysis overreacts to give several hydrazides while the reaction of hydrophilic X residues proceeds slowly. In this research, we attempted to develop an X-independent CPaseY-mediated protocol and found that the incorporation of a triple CP sequence into the C-terminal end (X-(CP)-Leu-OH) allows for efficient X-SR formation in a manner that is independent of X. (Keyword) carboxypeptidase / hydrazinolysis / native chemical ligation / protein semi-synthesis / protein thioester / thioesterification (Link to Publication Site) ● Publication site (DOI): 10.1248/cpb.c20-00674 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 33028801 ● Search Scopus @ Elsevier (PMID): 33028801 ● Search Scopus @ Elsevier (DOI): 10.1248/cpb.c20-00674 (DOI: 10.1248/cpb.c20-00674, PubMed: 33028801)
18.	Daishiroh Kobayashi, Naoto Naruse, Masaya Denda, Akira Shigenaga and Akira Otaka : Deprotection of S-Acetamidomethyl Cysteine with Copper (II) and 1,2-Aminothiols under Aerobic Conditions, Organic & Biomolecular Chemistry, Vol.18, 8638-8645, 2020. (Tokushima University Institutional Repository) ● Metadata: 115115 (Link to Publication Site) ● Publication site (DOI): 10.1039/D0OB01475C (Link to Search Site for Scientific Articles) ● Search Scopus @ Elsevier (DOI): 10.1039/D0OB01475C (Tokushima University Institutional Repository: 115115, DOI: 10.1039/D0OB01475C)
19.	Kento Ohkawachi, Daishiroh Kobayashi, Kyohei Morimoto, Akira Shigenaga, Masaya Denda, Kenzo Yamatsugu, Motomu Kanai and Akira Otaka : Sulfanylmethyldimethylaminopyridine as a Useful Thiol Additive for Ligation Chemistry in Peptide/Protein Synthesis, Organic Letters, Vol.22, No.14, 5289-5293, 2020. (Summary) Sulfanylmethyl-installed dimethylaminopyridine, 2-sulfanylmethyl-4-dimethylaminopyridine (), has an acidic thiol group comparable to that in aryl thiols due to the formation of a zwitterion consisting of a thiolate anion and a pyridinium cation. It can be used as an additive for native chemical ligation. The alkyl thiol in allows it to be used for the one-pot native chemical ligation-desulfurization protocol in peptide synthesis. The utility of in the synthesis of cyclic peptides is demonstrated. (Tokushima University Institutional Repository) ● Metadata: 114733 (Link to Publication Site) ● Publication site (DOI): 10.1021/acs.orglett.0c01383 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 32396369 ● Search Scopus @ Elsevier (PMID): 32396369 ● Search Scopus @ Elsevier (DOI): 10.1021/acs.orglett.0c01383 (Tokushima University Institutional Repository: 114733, DOI: 10.1021/acs.orglett.0c01383, PubMed: 32396369)
20.	Yunpeng Zhang, Atsushi Yonezawa, Shunsaku Nakagawa, Satoshi Imai, Masaya Denda, Tomohiro Omura, Takayuki Nakagawa and Kazuo Matsubara : Cisplatin, rather than oxaliplatin, increases paracellular permeability of LLC-PK1 cells via activating protein kinase C., Drug Metabolism and Pharmacokinetics, Vol.35, No.1, 111-116, 2019. (Summary) The clinical use of cisplatin is limited by its adverse events, particularly serious nephrotoxicity. It was clarified that cisplatin is transported by a kidney-specific organic cation transporter (OCT2). OCT2 also mediates the uptake of oxaliplatin into renal proximal tubular cells; however, this agent does not lead nephrotoxicity. In the present study, we carried out comparative experiments with cisplatin and oxaliplatin using porcine kidney LLC-PK1 cell monolayers. In the fluorescein-labeled isothiocyanate-dextran flux assay, the basolateral application of cisplatin, but not oxaliplatin, resulted in an increase in the paracellular permeability of cell monolayers. Even though the cellular accumulation of platinum at 50 μM oxaliplatin could reach the same level at 30 μM cisplatin, oxaliplatin did not induce hyper-permeability in cell monolayers. Cisplatin, but not oxaliplatin, significantly activated PKC. In addition, the combination of PKC inhibitors recovered the increase in paracellular permeability. In conclusion, pharmacodynamic mechanisms via PKC could explain the difference in nephrotoxicity between cisplatin and oxaliplatin. (Link to Publication Site) ● Publication site (DOI): 10.1016/j.dmpk.2019.09.001 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 31964622 ● Summary page in Scopus @ Elsevier: 2-s2.0-85077914257 (DOI: 10.1016/j.dmpk.2019.09.001, PubMed: 31964622, Elsevier: Scopus)
21.	Atushi Yonezawa, Yuki Otani, Toshiyuki Kitano, Mayuko Mori, Sho Masui, Yui Isomoto, Masahiro Tsuda, Satoshi Imai, Yasuaki Ikemi, Masaya Denda, Yuki Sato, Shunsaku Nakagawa, Tomohiro Omura, Takayuki Nakagawa, Ikuko Yano, Makoto Hayakari, Akifumi Takaori-Kondo and Kazuo Matsubara : Concentration and Glycoform of Rituximab in Plasma of Patients with B Cell Non-Hodgkin's Lymphoma., Pharmaceutical Research, Vol.36, No.6, 82, 2019. (Summary) Inter-individual variations in plasma concentrations of rituximab were found in some B-NHL patients. We could analyze a change in glycoforms of rituximab in the patients, and this finding may affect the pharmacokinetics of rituximab. (Keyword) Adult / Aged / Antineoplastic Agents / B-Lymphocytes / female / Glycoproteins / Humans / Lymphoma, Non-Hodgkin / male / Middle Aged / plasma / Protein Conformation / Rituximab (Link to Publication Site) ● Publication site (DOI): 10.1007/s11095-019-2624-5 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 30989405 ● CiNii @ National Institute of Informatics (CRID): 1050845763182203520 ● Summary page in Scopus @ Elsevier: 2-s2.0-85064466569 (DOI: 10.1007/s11095-019-2624-5, PubMed: 30989405, CiNii: 1050845763182203520, Elsevier: Scopus)

Academic Paper (Unrefereed Paper):

1.	Kohta Hidaka, JUNYA Hayashi, Daishiro Kobayashi, Masaya Denda and Akira Otaka : Advanced Insulin Synthesis by One-pot/stepwise Disulfide Bond Formation Enabled by Acid-activated S-Protected Cysteine Sulfoxide in the Presence of Chloride Anion, ChemRxiv, 2024. (Link to Publication Site) ● Publication site (DOI): 10.26434/chemrxiv-2024-jg5z3 (Link to Search Site for Scientific Articles) ● Search Scopus @ Elsevier (DOI): 10.26434/chemrxiv-2024-jg5z3 (DOI: 10.26434/chemrxiv-2024-jg5z3)
2.	Daishiroh Kobayashi, Masaya Denda, JUNYA Hayashi, Kohta Hidaka, Yutaka Kohmura, Takaaki Tsunematsu, Kohei Nishino, Harunori Yoshikawa, OHKAWACHI Kento, Kiyomi Nigorikawa, Tetsuro Yoshimaru, Naozumi Ishimaru, Nomura Wataru, Toyomasa Katagiri, Hidetaka Kosako and Akira Otaka : Sulfoxide-mediated Cys-Trp-selective bioconjugation that enables protein labeling and peptide heterodimerization, ChemRxiv, 2024. (Link to Publication Site) ● Publication site (DOI): 10.26434/chemrxiv-2024-tkv7w-v2 (Link to Search Site for Scientific Articles) ● Search Scopus @ Elsevier (DOI): 10.26434/chemrxiv-2024-tkv7w-v2 (DOI: 10.26434/chemrxiv-2024-tkv7w-v2)
3.	Kaito Anzaki, OHKAWACHI Kento, Daishiroh Kobayashi, Kyan Ryuji, Masaya Denda, Akira Shigenaga and Akira Otaka : Residue-Specific Modification Reaction Using S-Acetamidomethyl Cysteine Sulfoxide, Cys(Acm)(O), Peptide Science 2021, 55-56, 2022.
4.	Daishiroh Kobayashi, Yutaka Kohmura, Junya Hayashi, Masaya Denda and Akira Otaka : Development of copper and iron-mediated Cys-Trp-linking reaction, Peptide Science 2021, 9-12, 2022.
5.	OHKAWACHI Kento, Daishiroh Kobayashi, Kyohei Morimoto, Akira Shigenaga, Masaya Denda, Kenzo Yamatsugu, Motomu Kanai and Akira Otaka : A New Thiol Additive for One-pot Sequential Peptide Ligation-Desulfurization Chemistry, Peptide Science 2020, 25-26, 2021.
6.	Daishiroh Kobayashi, Naoto Naruse, Masaya Denda, Akira Shigenaga and Akira Otaka : Deprotection of S-Acetamidomethyl Cysteine Mediated by Copper Salts, Peptide Science 2020, 49-52, 2021.

Review, Commentary:

1.	Masaya Denda and Akira Otaka : Advances in Preparation of Peptide and Protein Thioesters Aiming to Use in Medicinal Sciences, Chemical & Pharmaceutical Bulletin, Vol.70, No.5, 316-323, May 2022. (Link to Publication Site) ● Publication site (DOI): 10.1248/cpb.c21-01019 (Link to Search Site for Scientific Articles) ● Search Scopus @ Elsevier (DOI): 10.1248/cpb.c21-01019 (DOI: 10.1248/cpb.c21-01019)

Proceeding of International Conference:

1.	SATOH Daiki, Chiho Shinozaki, Masaya Denda and Akira Otaka : Development of late-stage acylation methodology of threonine residue enabled by chemoselective acyl transfer followed by desulfurization, 37th European Peptide Symposium 14th International Peptide Symposium, Firenze, Aug. 2024.
2.	Kohta Hidaka, Daishiro Kobayashi, JUNYA Hayashi, Masaya Denda and Akira Otaka : Disulfide-shuffling encountered in insulin synthesis using disulfide-forming reaction enabled by S-protected cysteine and sulfoxide pair, 9th Chemical Protein Synthesis Conference, Nagoya, Jun. 2024.
3.	JUNYA Hayashi, Daishiro Kobayashi, Masaya Denda and Akira Otaka : Development of α-thioetherification reaction on peptides for sactipeptide synthesis using glycyl hydroxamic acid, 9th Chemical Protein Synthesis Conference, Nagoya, Jun. 2024.
4.	SATOH Daiki, Chiho Shinozaki, Masaya Denda and Akira Otaka : Development of acylation protocol of threonine residue by sequential highly efficient acyl transfersdesulfurization, 9th Chemical Protein Synthesis Conference, Nagoya, Jun. 2024.
5.	Akira Otaka, Kohta Hidaka, Daishiro Kobayashi, JUNYA Hayashi and Masaya Denda : Insulin Synthesis Using Stepwise Disulfide Bond Formation Enabled by S-Protected Cysteine and Cysteine Sulfoxide Pairs, 9th Chemical Protein Synthesis Conference, Nagoya, Jun. 2024.
6.	Daishiro Kobayashi, Masaya Denda and Akira Otaka : S-Protected cysteine sulfoxide-enabled peptide and protein customization methodology, Biologics 2024, London, Mar. 2024.
7.	Kohta Hidaka, Daishiro Kobayashi, JUNYA Hayashi, OHKAWACHI Kento, Masaya Denda and Akira Otaka : DEVELOPMENT OF ONE-POT/STEPWISE DISULFIDE BOND-FORMING REACTION ENABLED BY S-PROTECTED CYSTEINE SULFOXIDE WITH ITS APPLICATION TO SYNTHESIS OF INSULIN AND ITS LIPIDATED ANALOGUE, 13th International Peptide Symposium 15th Australian Peptide Conference, Brisbane, Oct. 2023.
8.	JUNYA Hayashi, Daishiro Kobayashi, Masaya Denda and Akira Otaka : DEVELOPMENT OF OXIDANT FREE METHODOLOGY FOR PREPARING N-GLYOXYLYL PEPTIDE AND ITS APPRICATIONS, 13th International Peptide Symposium 15th Australian Peptide Conference, Brisbane, Oct. 2023.
9.	Daishiro Kobayashi, JUNYA Hayashi, Kohta Hidaka, OHKAWACHI Kento, Yutaka Kohmura, Masaya Denda and Akira Otaka : Protein tryptophan modification enabled by using S-protected cysteine sulfoxide under mild acid conditions, 13th International Peptide Symposium 15th Australian Peptide Conference, Brisbane, Oct. 2023.
10.	Mika Ohhira, OHKAWACHI Kento, Kaito Anzaki, Mina Hojo, Sayaka Tani, Masaya Denda, Hitoshi Mizuguchi and Akira Otaka : Development of synthetic method for synthesizing di-Tyr-containing bi-aryl peptides enabled by oxidation of sulfenyl Tyr, AIMECS 2023, Seoul, Jun. 2023.
11.	Chiho Shinozaki, Yutaka Kohmura, Tetsuro Yoshimaru, Tsuyoshi Tahara, Masaya Denda, Hidefumi Mukai, Kohta Mohri, Yi Long Chen, Toyomasa Katagiri and Akira Otaka : Study on a lipidated anti-cancer peptide allowing long-lasting duration in mice model, AIMECS 2023, Seoul, Jun. 2023.
12.	Akira Otaka, OHKAWACHI Kento, Kaito Anzaki and Masaya Denda : Tyr- or Trp-selective CH sulfenylation enabled by acid- activated S-acetamidomethyl cysteine sulfoxide, 19th Akabori Conference German-Japanese Symposium on Peptide Science, 大津市, May 2023.

Proceeding of Domestic Conference:

1.	SASAGAWA Daiki, Chiho Shinozaki, Masaya Denda, Tetsuro Yoshimaru, Toyomasa Katagiri and Akira Otaka : アミド型側鎖架橋を有する乳がん増殖抑制ペプチドの改良合成法の開発, 日本薬学会第145年会, Mar. 2025.
2.	JUNYA Hayashi, Masaya Denda and Akira Otaka : N-ヒドロキシペプチドを足掛かりとした新規ペプチドフラグメント縮合法の開発, 日本薬学会第145年会, Mar. 2025.
3.	INAZUKI Hayato, Takashi Tsuji, Daishiro Kobayashi, HAYASHI Junya, Masaya Denda and Akira Otaka : Cysteinylprolyl ester を利用した脂肪鎖―薬物複合体からの薬物放出システムの開発研究, 第41回メディシナルケミストリーシンポジウム, Nov. 2024.
4.	Kohta Hidaka, Daishiro Kobayashi, HAYASHI Junya, Masaya Denda and Akira Otaka : SELENAZOLIDINE AS A DUALLY FUNCTIONING AGGREGATION DISRUPTING UNIT, 第61回ペプチド討論会, Oct. 2024.
5.	NAGATA Tsunaki, Daishiro Kobayashi, Masaya Denda and Akira Otaka : S-保護CysスルホキシドによるTrp選択的スルフェニル化反応を利用したGIP–GLP-1ヘテロダイマー合成, 創薬懇話会2024 札幌, Jun. 2024.
6.	EGUCHI Aki, OHKAWACHI Kento, Mika Ohhira, Masaya Denda and Akira Otaka : 人工脂質膜を反応場とした難溶性膜タンパク質化学合成法の開発, 創薬懇話会2024 札幌, Jun. 2024.
7.	OHTA Rika, SATOH Daiki, Masaya Denda and Akira Otaka : 新規スレオニン側鎖アシル化法を用いた刺激応答性機能変換ペプチドの合成, 日本ケミカルバイオロジー学会第18回年会, May 2024.
8.	JUNYA Hayashi, Daishiro Kobayashi, Masaya Denda and Akira Otaka : 主鎖アミド保護基を活用したLossen転位反応による合成後期ペプチドα位ヘテロ化法の開発, 日本薬学会第144年会, Mar. 2024.
9.	Akiko Higashiyama, Akito Ohnishi, Shunya Yanagawa, 清良尚史, W John Regan, OHKAWACHI Kento, Masaya Denda, Keijo Fukushima, 西野耕平, Akira Otaka, Hidetaka Kosako and Hiromichi Fujino : EP4受容体の細胞内第3ループ領域に相互作用する因子の探索, 日本薬学会第144年会,横浜,2024年3月29日, 2024.
10.	Chiho Shinozaki, Yutaka Kohmura, Tetsuro Yoshimaru, Masaya Denda, Toyomasa Katagiri and Akira Otaka : 脂肪酸修飾型乳がん増殖抑制ペプチドの開発, 第40回メディシナルケミストリーシンポジウム, Nov. 2023.
11.	Kohta Hidaka, Daishiro Kobayashi, JUNYA Hayashi, OHKAWACHI Kento, Masaya Denda and Akira Otaka : 脂肪鎖修飾型インスリン誘導体合成を指向したS-保護システインスルホキシドを利用したワンポットジスルフィド形成/脂肪酸修飾法の開発, 第40回メディシナルケミストリーシンポジウム, Nov. 2023.
12.	Kohta Hidaka, Daishiro Kobayashi, JUNYA Hayashi, OHKAWACHI Kento, Masaya Denda and Akira Otaka : IMPROVEMENT OF INSULIN SYNTHESIS BY COMBINATION OF O-ACYL ISOPEPTIDE METHOD AND ONE-POT/STEPWISE DISULFIDE BOND FORMATION USING S-PROTECTED CYSTEINE SULFOXIDE, 第60回ペプチド討論会, Nov. 2023.
13.	Mika Ohhira, OHKAWACHI Kento, Kaito Anzaki, Sayaka Tani, Mina Hojo, Masaya Denda, Hitoshi Mizuguchi and Akira Otaka : DEVELOPMENT OF SYNTHETIC METHOD FOR DI-TYR CONTAINING PEPTIDES RELATED TO PARKINSONS DISEASE ENABLED BY OXIDATION SULFENYL TYR, 第60回ペプチド討論会, Nov. 2023.
14.	Daiki Sato, Chiho Shinozaki, Masaya Denda and Akira Otaka : DEVELOPMENT OF INTERMOLECULAR ACYLATION PROTOCOL OF THREONINE BY A LATE-STAGE SEQUENTIAL ACYL TRANSFER DESULFURIZATION, 第60回ペプチド討論会, Nov. 2023.
15.	Daishiro Kobayashi, JUNYA Hayashi, Kohta Hidaka, OHKAWACHI Kento, Yutaka Kohmura, Masaya Denda and Akira Otaka : TRYPTOPHAN-SELECTIVE PEPTIDE MODIFICATION USING S-ACETAMIDEMETHYL PROTECTED CYSTEINE SULFOXIDE UNDER MILD ACIDIC CONDITION AND ITS APPLICATION TO PEPTIDE HETERODIMERIZATION, 第60回ペプチド討論会, Nov. 2023.
16.	JUNYA Hayashi, Daishiro Kobayashi, Masaya Denda and Akira Otaka : PREPARATION METHODOLOGY OF N-GLYOXYLYL PEPTIDE UTILIZING LOSSEN REARRANGEMENT, 第60回ペプチド討論会, Nov. 2023.
17.	JUNYA Hayashi, Daishiroh Kobayashi, Masaya Denda and Akira Otaka : Lossen転位を利用したペプチドN末端アルデヒド化法の開発と応用, 第49回反応と合成の進歩シンポジウム, Nov. 2023.
18.	Daishiroh Kobayashi, JUNYA Hayashi, Kohta Hidaka, Yutaka Kohmura, OHKAWACHI Kento, Masaya Denda and Akira Otaka : Interrupted Pummerer反応によるTrp選択的修飾を利用したOne-potペプチドヘテロ二量化法の開発, 第49回反応と合成の進歩シンポジウム, Nov. 2023.
19.	OHTA Rika, SATOH Daiki, Masaya Denda and Akira Otaka : 刺激応答性機能変換ペプチドの新規合成法の開発, 第62回日本薬学会・日本薬剤師会・日本病院薬剤師会中国四国支部学術大会, Oct. 2023.
20.	EGUCHI Aki, OHKAWACHI Kento, Mika Ohhira, Masaya Denda and Akira Otaka : 脂質ナノディスクを利用した難溶解性膜タンパク質化学合成法の開発, 第62回日本薬学会・日本薬剤師会・日本病院薬剤師会中国四国支部学術大会, Oct. 2023.
21.	INAZUKI Hayato, Takashi Tsuji, Daishiro Kobayashi, JUNYA Hayashi, Masaya Denda and Akira Otaka : Cysteinyl Prolyl Esterシステムを利用した新規医薬品放出制御システムの開発研究, 第62回日本薬学会・日本薬剤師会・日本病院薬剤師会中国四国支部学術大会, Oct. 2023.
22.	NAGATA Tsunaki, Tomoki Nonaka, Daishiro Kobayashi, Masaya Denda and Akira Otaka : Cys(MBzl)(O)を利用したTrp位置選択的脂肪鎖修飾法の開発と修飾GIP調製への応用, 第62回日本薬学会・日本薬剤師会・日本病院薬剤師会中国四国支部学術大会, Oct. 2023.
23.	Kohta Hidaka, Daishiro Kobayashi, JUNYA Hayashi, OHKAWACHI Kento, Masaya Denda and Akira Otaka : 保護システインスルホキシドを用いたワンポット連続ジスルフィド形成によるインスリンの合成研究, 創薬懇話会2023 湯河原, Jun. 2023.
24.	Daiki Satoh, Chiho Shinozaki, Masaya Denda and Akira Otaka : ユビキチン化の機能解明を志向した新規スレオニン側鎖アシル化法の開発, 日本ケミカルバイオロジー学会第17回年会, May 2023.
25.	Masaya Denda, Tomoki Nonaka, Daishiro Kobayashi, JUNYA Hayashi, Yasuda Takuma, Yutaka Kohmura, Harada Norio, Inagaki Nobuya and Akira Otaka : S-保護システインスルホキシドを利用したトリプトファン選択的修飾法の開発, 日本ケミカルバイオロジー学会第17回年会, May 2023.
26.	OHKAWACHI Kento, Kaito Anzaki, Daishiro Kobayashi, 喜屋武龍二, Masaya Denda, Akira Shigenaga and Akira Otaka : S-保護システインスルホキシドを利用した残基選択的C-Hスルフェニル化反応の開発, 日本薬学会第143年会, Mar. 2023.
27.	Daiki Satoh, Chiho Shinozaki, Masaya Denda and Akira Otaka : 連続アシル転移を利用した分子内および分子間スレオニン側鎖アシル化法の開発, 日本薬学会第143年会, Mar. 2023.
28.	Kohki Fukuhara, Tsubasa Inokuma, MASUI Kana, Masaya Denda, Akira Otaka and Ken-ichi Yamada : N-2-Nitrophenylsulfenylイミノペプチドへのジアステレオ選択的インドリル化反応の開発, 日本薬学会第143年会, Mar. 2023.
29.	JUNYA Hayashi, Daishiroh Kobayashi, Masaya Denda and Akira Otaka : アシルイミニウムカチオンを経由したペプチド主鎖修飾反応の開発, 第48回反応と合成の進歩シンポジウム, Nov. 2022.
30.	Tomoki Nonaka, Daishiro Kobayashi, KURAOKA Eisuke, JUNYA Hayashi, Yasuda Takuma, Yutaka Kohmura, Masaya Denda, Harada Norio, Inagaki Nobuya and Akira Otaka : S-保護システインスルホキシドを利用したトリプトファン選択的脂肪鎖修飾法の開発と応用, 第39回メディシナルケミストリーシンポジウム, Nov. 2022.
31.	Mika Ohhira, OHKAWACHI Kento, Kaito Anzaki, Mina Hohjoh, Hitoshi Mizuguchi, Masaya Denda and Akira Otaka : スルフェニル化Tyrを利用したTyr-Tyrビアリール構造含有ペプチド合成法の開発, 第61回日本薬学会・日本薬剤師会・日本病院薬剤師会中国四国支部学術大会, Nov. 2022.
32.	Kohta Hidaka, Daishiro Kobayashi, JUNYA Hayashi, OHKAWACHI Kento, Masaya Denda and Akira Otaka : S-保護システインスルホキシドを利用したトリプトファン選択的修飾反応の開発とペプチドヘテロ二量化法への応用展開, 第61回日本薬学会・日本薬剤師会・日本病院薬剤師会中国四国支部学術大会, Nov. 2022.
33.	Tsubasa Inokuma, MASUI Kana, Masaya Denda, Akira Otaka and Ken-ichi Yamada : Diastereoselective indolylation of N-2-nitrophenylsulfenyl iminopeptide for the synthesis of α-indolylglycine-containing peptide, 第59回ペプチド討論会, Oct. 2022.
34.	Kohta Hidaka, Daishiro Kobayashi, JUNYA Hayashi, OHKAWACHI Kento, Masaya Denda and Akira Otaka : DEVELOPMENT OF ONE-POT/STEPWISE DISULFIDE BOND-FORMING REACTION ENABLED BY S-PROTECTED CYSTEINE SULFOXIDE WITH ITS APPLICATION TO INSULIN SYNTHESIS, 第59回ペプチド討論会, Oct. 2022.
35.	JUNYA Hayashi, Daishiro Kobayashi, Masaya Denda and Akira Otaka : DEVELOPMENT OF INTRAMOLECULAR THIOETHERIFICATION ON PEPTIDE BACKBONE FOR CHEMICAL SYNTHESIS OF SACTIPEPTIDE, 第59回ペプチド討論会, Oct. 2022.
36.	JUNYA Hayashi, Daishiroh Kobayashi, Masaya Denda and Akira Otaka : ペプチド主鎖修飾反応の開発とチオエーテル含有環状ペプチド合成への展開, 第54回若手ペプチド夏の勉強会, Aug. 2022.
37.	Daishiroh Kobayashi, JUNYA Hayashi, Kohta Hidaka, OHKAWACHI Kento, Yutaka Kohmura, Masaya Denda and Akira Otaka : 保護システインスルホキシドを利用したペプチド・タンパク質Trp残基選択的修飾法の開発研究, 第54回若手ペプチド夏の勉強会, Aug. 2022.
38.	JUNYA Hayashi, Daishiroh Kobayashi, Masaya Denda and Akira Otaka : Lossen転位を起点とした合成後期ペプチド主鎖ヘテロ化反応の開発, 創薬懇話会2022 in 名古屋, Jul. 2022.
39.	Daishiroh Kobayashi, KURAOKA Eisuke, Yutaka Kohmura, Junya Hayashi, Masaya Denda and Akira Otaka : S-保護システインスルホキシドを利用したトリプトファン選択的修飾反応の開発研究, 日本薬学会第142年会, Mar. 2022.
40.	Yutaka Kohmura, Daishiroh Kobayashi, Masaya Denda and Akira Otaka : MBzl保護システインスルホキシドの芳香族化合物に対する反応性評価とペプチド架橋法への応用展開, 日本薬学会第142年会, Mar. 2022.
41.	SATOH Daiki, Honoka Tsunematsu, Isamu Konishi, UEDA Tomoko, Chiaki Komiya, Masaya Denda, Akira Shigenaga and Akira Otaka : 側鎖無保護ペプチドへの適用可能な合成後期ラクトン化法の開発, 日本薬学会第142年会, Mar. 2022.
42.	Akito Ohnishi, Akiko Higashiyama, Shunya Yanagawa, 清良尚史, W John Regan, Kento Ohkawachi, Masaya Denda, Keijo Fukushima, Akira Otaka and Hiromichi Fujino : プロスタノイドEP4受容体の1アミノ酸変異によるシグナル伝達プロファイル変化, 第95回日本薬理学会年会，福岡, Mar. 2022.
43.	Kaito Anzaki, OHKAWACHI Kento, Daishiroh Kobayashi, 喜屋武龍二, Masaya Denda, Akira Shigenaga and Akira Otaka : RESIDUE-SPECIFIC MODIFICATION REACTION USING S-ACETAMIDOMETHYL CYSTEINE SULFOXIDE, Cys(Acm)(O), 第58回ペプチド討論会, Oct. 2021.
44.	Daishiroh Kobayashi, Yutaka Kohmura, Junya Hayashi, Masaya Denda and Akira Otaka : Development of copper and iron-mediated Cys-Trp-linking reaction, 第58回ペプチド討論会, Oct. 2021.
45.	Daishiroh Kobayashi, Yutaka Kohmura, Junya Hayashi, Masaya Denda and Akira Otaka : 銅添加を鍵としたシステイン-トリプトファン間架橋反応の開発研究, 第53回若手ペプチド夏の勉強会, Aug. 2021.
46.	Tomoki Nonaka, Kento Ohkawachi, Masaya Denda and Akira Otaka : Sulfanylmethyl DMAPを利用した環状ペプチド合成に関する研究, 第53回若手ペプチド夏の勉強会, Aug. 2021.
47.	Kaito Anzaki, Kento Ohkawachi, Daishiroh Kobayashi, 喜屋武龍二, Masaya Denda, Akira Shigenaga and Akira Otaka : Acm 保護 Cys スルホキシドを利用した化学選択的 S-Aryl 化反応開発研究, 第53回若手ペプチド夏の勉強会, Aug. 2021.
48.	Kaito Anzaki, Kento Ohkawachi, Daishiroh Kobayashi, 喜屋武龍二, Masaya Denda, Akira Shigenaga and Akira Otaka : 保護Cysスルホキシドを利用したS–Aryl化環状ペプチド合成研究, 創薬懇話会2021 in 京都, Jun. 2021.
49.	Yutaka Kohmura, Daishiroh Kobayashi, 杉木俊彦, Tetsuro Yoshimaru, Eisuke Kuraoka, Masaya Denda, 藤原敏道, Toyomasa Katagiri and Akira Otaka : Cys-Trp 架橋型乳がん抑制ペプチド(ERAP)の合成及び活性評価, 創薬懇話会2021 in 京都, Jun. 2021.
50.	Masaya Denda, Chiaki Komiya, Masahiro Ueda, Jun Tsukimoto, Kouji Itou, Akira Shigenaga and Akira Otaka : 既存モダリティの高度化を指向したペプチド・タンパク質新規修飾法の開発, 日本薬剤学会第36年会, May 2021.
51.	SATOH Daiki, Honoka Tsunematsu, UEDA Tomoko, Chiaki Komiya, Masaya Denda, Akira Shigenaga and Akira Otaka : 側鎖無保護ペプチドを用いた環状デプシペプチド簡便合成法の開発, 日本薬学会第141年会, Mar. 2021.
52.	Daishiroh Kobayashi, Yutaka Kohmura, KURAOKA Eisuke, Masaya Denda and Akira Otaka : S-保護システインスルホキシドを利用したCys-Trpチオエーテル結合形成反応の開発, 日本薬学会第141年会, Mar. 2021.
53.	Daiki Satoh, Honoka Tsunematsu, Tomoko Ueda, Chiaki Komiya, Masaya Denda, Akira Shigenaga and Akira Otaka : Development of a protection-free protocol for the synthesis of lactone peptides, 第57回ペプチド討論会, Nov. 2020.
54.	Daishiroh Kobayashi, Naoto Naruse, Masaya Denda, Akira Shigenaga and Akira Otaka : Deprotection of S-acetamidomethyl cysteine mediated by copper salts, 第57回ペプチド討論会, Nov. 2020.
55.	Kento Ohkawachi, Daishiroh Kobayashi, Kyohei Morimoto, Akira Shigenaga, Masaya Denda, Kenzo Yamatsugu, Motomu Kanai and Akira Otaka : A new thiol additive for one-pot sequential peptide ligation-desulfurization chemistry, 第57回ペプチド討論会, Nov. 2020.

Et cetera, Workshop:

1.	Tsuyoshi Tahara, Chiho Shonozaki, Tetsuro Yoshimaru, 毛利浩太, Masaya Denda, Tamaki Otani, Toyomasa Katagiri, Akira Otaka, 向井英史 and 崔翼龍 : Kinetic analysis for lapidated anti-cancer peptides using PET, 日本分子イメージング学会, May 2024.

Grants-in-Aid for Scientific Research (KAKEN Grants Database @ NII.ac.jp)

相互作用タンパク質の同定・トポロジー解析を指向した光活性型クロスリンカーの開発 (Project/Area Number: 24K09728 )
Development of a method for modifying peptides using cation-generating sulfoxides (Project/Area Number: 23K27300 )
ペプチド環化反応をトリガーとした抗がん剤新規放出システム搭載型ADCの創出研究 (Project/Area Number: 22K15253 )
TDM解析を基盤とした、リウマチ治療における生物学的製剤適正使用法の確立研究 (Project/Area Number: 19K16445 )
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Assistant Professor : Denda, Masaya

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Grants-in-Aid for Scientific Research (KAKEN Grants Database @ NII.ac.jp)