研究者詳細 - 前田　衣織

論文 - 前田　衣織

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Development of the efficient preparation method for thermoresponsive elastin-like peptides using liquid-phase synthesis combined with fragment condensation strategy 査読有り国際誌

Yoshida K., Suyama K., Matsushita S., Maeda I., Nose T.

J Pept Sci 29 ( 12 ) e3528 2023年12月

記述言語：英語掲載種別：研究論文（学術雑誌）

Elastin-like peptides (ELPs) are synthetic peptides that mimic the characteristic hydrophobic amino acid repeat sequences of elastin and exhibit temperature-dependent reversible self-assembly properties. ELPs are expected to be used as temperature-responsive biomolecular materials across diverse industrial and research fields, and there is a requirement for a straightforward method to mass-produce them. Previously, we demonstrated that phenylalanine-containing ELP analogs, namely, (FPGVG)n , can undergo coacervation with short chains (n = 5). The Fmoc solid-phase peptide synthesis method is one strategy used to synthesize these short ELPs. However, owing to its low reaction efficiency, an efficient method for preparing ELPs is required. In this study, efficient preparation of ELPs was investigated using a liquid-phase synthesis method with a hydrophobic benzyl alcohol support (HBA-tag). Because HBA-tags are highly hydrophobic, they can be easily precipitated by the addition of poor solvents and recovered by filtration. This property allows the method to combine the advantages of the simplicity of solid-phase methods and the high reaction efficiency of liquid-phase methods. By utilizing liquid-phase fragment condensation with HBA-tags, short ELPs were successfully obtained in high yield and purity. Finally, the temperature-dependent response of the ELPs generated through fragment condensation was assessed using turbidity measurements, which revealed a reversible phase transition. Consequently, the ELPs exhibited a reversible phase transition, indicating successful synthesis of ELPs via fragment preparation with tags. These findings provide evidence of the potential for mass production of ELPs using this approach.

DOI： 10.1002/psc.3528

その他リンク： https://pubmed.ncbi.nlm.nih.gov/37340996/

Enhancement of Aggregate Formation Through Aromatic Compound Adsorption in Elastin-like Peptide (FPGVG)<inf>5</inf> Analogs 査読有り

Suyama K., Murashima M., Maeda I., Nose T.

Biomacromolecules 24 ( 11 ) 5265 - 5276 2023年11月

記述言語：英語掲載種別：研究論文（学術雑誌）

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.

DOI： 10.1021/acs.bio mac.3c00779

その他リンク： https://pubmed.ncbi.nlm.nih.gov/37865930/

Determining the Sequence Dependency of Self-Assembly of Elastin-Like Peptides Using Short Peptide Analogues with Shuffled Repetitive Sequences 査読有り国際誌

Tatsubo D., Suyama K., Sakamoto N., Tomohara K., Taniguchi S., Maeda I., Nose T.

Biochemistry 62 ( 17 ) 2559 - 2570 2023年09月

記述言語：英語掲載種別：研究論文（学術雑誌）

Synthetic elastin-like peptides (ELPs) that possess characteristic tropoelastin-derived hydrophobic repetitive sequences, such as (VPGVG)n, exhibit thermoresponsive reversible self-assembly. Although their thermoresponsive properties have been well-studied, the sequence-dependent and structural requirements for self-assembly remain ambiguous. In particular, it is still unclear whether the amino acid sequences derived from tropoelastin are necessary for self-assembly. In this study, 11 sequence-shuffled ELP analogues based on (FPGVG)5, which is a previously developed short ELP (sELP), were designed to elucidate the sequence-dependent and structural requirements for their self-assembly. Among them, eight shuffled peptides exhibited self-assembling properties, whereas the other three peptides were difficult to dissolve in water. Structural analyses revealed that the structural characteristics of the three insoluble peptides were different from those of their thermoresponsive analogues. Furthermore, the secondary structures of the peptide analogues possessing the self-assembly abilities were different from each other. These results suggest that the potential for self-assembly and water solubility of sELPs depend on the primary structure in each repeated unit. Moreover, several shuffled analogues exhibited more potent self-assembling properties than the original (FPGVG)5, indicating that shorter ELPs can be obtained using their novel motifs as repetitive units. We also observed that the presence of Pro-Gly sequence in the repeating units was advantageous in terms of peptide solubility. Although further analysis will be necessary to elucidate the molecular mechanism underlying the self-assembly of these sELPs, this study provides insights into the relationship between the amino acid sequence and the self-assembling ability of the peptides for developing new sELPs for various applications.

DOI： 10.1021/acs.biochem.3c00146

その他リンク： https://pubs.acs.org/doi/10.1021/acs.biochem.3c00146

Aromatic compounds scavenging ability of thermo-responsive short elastin-like peptide (FPGVG)n analogs 査読有り国際誌

Keitaro Suyama ,Masayuki Murashima,Iori Maeda ,Takeru Nose

Peptide Science 2022 ( 日本ペプチド学会 ) 25 - 26 2023年03月

Branched short elastin-like peptides with temperature responsiveness obtained by EDTA-mediated multimerization 査読有り国際誌

Tanaka N., Suyama K., Tomohara K., Maeda I., Nose T.

J Pept Sci 29 ( 2 ) e3449 p.1-10 2023年02月

記述言語：英語掲載種別：研究論文（学術雑誌）

Elastin-like peptides (ELPs) exhibit a reversible phase transition, known as coacerva- tion, triggered by temperature changes. This property makes them useful as stimuli- responsive molecular materials for various applications. Among ELPs, short peptide chain lengths have some advantages over long peptide chain lengths because short ELPs can be easily obtained by chemical synthesis, allowing the use of various amino acids, including D-type and unnatural amino acids, at any position in the sequence. Moreover, the incorporated amino acids readily affect the temperature-responsive behavior of ELPs. However, to be utilized in various applications, it is necessary to develop short ELPs and to investigate their temperature-responsive properties. To obtain further insights into the temperature-responsive behavior of the short ELPs, we investigated branched short ELP analogs composed of (FPGVG)n chains (n = 1 or 2, abbreviated as F1 and F2, respectively). We synthesized multimers composed of four F1 chains or two to four F2 chains using ethylenediaminetetraacetic acid (EDTA) as a central component of multimerization. Our results show that the multimers obtained exhibited coacervation in aqueous solutions whereas linear F1 or F2 did not. Furthermore, the structural features of the obtained multimers were the same as those of linear (FPGVG)4. In this study, we demonstrated that molecules capable of coacervation can be obtained by multimerization of F1 or F2. The temperature- responsive molecules obtained using short ELPs make it possible to use them as easy-to-synthesize peptide tags to confer temperature responsiveness to various molecules, which will aid the development of temperature-responsive biomaterials with a wide variety of functions.

DOI： 10.1002/psc.3449

その他リンク： https://onlinelibrary.wiley.com/doi/epdf/10.1002/psc.3449

Suitability of high-molecular-weight tissue-derived elastin polypeptides and their particles as cosmetic biomaterials 査読有り国際誌

Sakai T., Sodemoto N., Inoue A., Taniguchi S., Maeda I., Hikima T.

J Pept Sci e3472 p.1-10 2022年12月

記述言語：英語掲載種別：研究論文（学術雑誌）

We aimed to determine the coacervation properties of high-molecular-weight (HMW) tissue-derived elastin (TDE) and to examine the potential use of TDE parti- cles as a cosmetic biomaterial. TDE solutions were filtered and divided into three fractions (1–3) according to the molecular weight of the elastin. The turbidity of frac- tion 2, which contained a large portion (58%) of HMW elastin polypeptides (>100 kDa), was measured under several pH values (3.0–11.0) and NaCl concentra- tions (0–1000 mM) to examine its coacervation ability. HMW TDE exhibited coacer- vation under the physiological conditions (temperature, pH, and NaCl concentration) of the skin surface. We performed inclusion and release experiments using three model chemicals with different molecular weights and measured the size and zeta potential of the fraction 3 particles to investigate the suitability of HMW elastin poly- peptides. Fraction 3, which contained a larger portion (64%) of HMW elastin poly- peptides, displayed a strong coacervation property at a phase transition temperature of 19.8 ± 0.1C. The inclusion ratio of the model chemical Biebrich Scarlet (BS) with a molecular weight of <600 was approximately 92.1 ± 0.7%. The release profiles of BS from the particles linearly increased and reached a plateau after 15 days. Moreover, the average size of the particles with BS was 474.2 ± 24.6 nm. The low-molecular- weight (LMW) elastin peptides have moisturizing and whitening functions for the skin. We concluded that TDE, as a mixture of HMW polypeptides and LMW pep- tides, can potentially serve as a multifunctional and effective cosmetic biomaterial.

DOI： 10.1002/psc.3472

その他リンク： https://pubmed.ncbi.nlm.nih.gov/36541737/

Development of truncated elastin-like peptide analogues with improved temperature-response and self-assembling properties 査読有り

Sumiyoshi S., Suyama K., Tanaka N., Andoh T., Nagata A., Tomohara K., Taniguchi S., Maeda I., Nose T.

Scientific Reports 12 ( 1 ) 2022年11月

記述言語：英語掲載種別：研究論文（学術雑誌）

Functional peptides, which are composed of proteinogenic natural amino acids, are expected to be used as biomaterials with minimal environmental impact. Synthesizing a functional peptide with a shorter amino acid sequence while retaining its function is a easy and economical strategy. Furthermore, shortening functional peptides helps to elucidate the mechanism of their functional core region. Truncated elastin-like peptides (ELPs) are peptides consisting of repetitive sequences, derived from the elastic protein tropoelastin, that show the thermosensitive formation of coacervates. In this study, to obtain shortened ELP analogues, we synthesized several (Phe-Pro-Gly-Val-Gly)n (FPGVG)n analogues with one or two amino acid residues deleted from each repeat sequence, such as the peptide analogues consisting of FPGV and/or FPG sequences. Among the novel truncated ELP analogues, the 16-mer (FPGV)4 exhibited a stronger coacervation ability than the 25-mer (FPGVG)5. These results indicated that the coacervation ability of truncated ELPs was affected by the amino acid sequence and not by the peptide chain length. Based on this finding, we prepared Cd2+-binding sequence-conjugated ELP analogue, AADAAC-(FPGV)4, and found that it could capture Cd2+. These results indicated that the 16-mer (FPGV)4 only composed of proteinogenic amino acids could be a new biomaterial with low environmental impact.

DOI： 10.1038/s41598-022-23940-0

Scopus

その他リンク： https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85141734638&origin=inward

Flexible customization of the self-assembling abilities of short elastin-like peptide Fn analogs by substituting N-terminal amino acids 査読有り国際誌

Suyama K., shimizu M., Maeda I., Nose T.

Biopolymers 113 ( 10 ) e23521 p.1-14 2022年10月

記述言語：英語掲載種別：研究論文（学術雑誌）

Elastin-like peptides (ELPs) are thermoresponsive biopolymers inspired by the characteristic repetitive sequences of natural elastin. As ELPs exhibit temperature-dependent reversible self-assembly, they are expected to be biocompatible thermoresponsive materials for drug delivery carriers. One of the most widely studied ELPs in this field is the repetitive pentapeptide, (VPGXG)n . We previously reported that phenylalanine-containing ELP (Fn) analogs, in which the former Val residue of the repetitive sequence (VPGVG)n is replaced by Phe, show coacervation with a short chain length (n = 5). Owing to their short sequences, Fn analogs are easily modified in amino acid sequences via simple chemical synthesis, and are useful for investigating the relationship between peptide sequences and temperature responsiveness. In this study, we developed Fn analogs by replacing Phe residue(s) with other amino acids or introducing another amino acid at the N-terminus. The temperature responsiveness of the Fn analogs changed drastically with the substitution of a single Phe residue, suggesting that aromatic amino acids play an important role in their self-assembly. In addition, the self-assembling ability of Fn was enhanced by increasing the bulkiness of the N-terminal amino acids. Therefore, the N-terminal residue was considered to be important for hydrophobicity-induced intermolecular interactions between the peptides during coacervation.

DOI： 10.1002/bip.23521

その他リンク： https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85104330108&origin=inward

Development of temperature-responsive peptides by EDTA-mediated multimerization of short (FPGVG)n chains 査読有り国際誌

Naoki Tanaka, Keitaro Suyama, Keisuke Tomohara, Iori Maeda, and Takeru Nose

Peptide Science 2021 ( 日本ペプチド学会 ) 83 - 84 2022年03月

Development of temperature-responsive short-chain peptide analogues based on elastin-like peptide FPGVG 査読有り国際誌

Keitaro Suyama ,Marin Shimizu ,Iori Maeda ,Takeru Nose

Peptide Science 2021 ( 日本ペプチド学会 ) 141 - 142 2022年03月

Metal ion scavenging activity of elastin-like peptide analogues containing a cadmium ion binding sequence 査読有り国際誌

Shogo Sumiyoshi,Keitaro Suyama,Daiki Tatsubo,Naoki Tanaka,Keisuke Tomohara,Suguru Taniguchi,Iori Maeda,Takeru Nose

Scientific Reports ( Nature Publishing group ) 12 ( 1861 ) 1 - 16 1861: Article number 2022年02月

Role of Phe residues in elastin-like peptide (FPGVG)5 on self-assembly properties 査読有り国際誌

Keitaro Suyama ,Marin Shimizu ,Iori Maeda ,Takeru Nose

Peptide Science 2020 ( 日本ペプチド学会 ) 59 - 60 2021年03月

Fractionation of Water-soluble Elastin from Pig Aorta by Coacervation Method 査読有り国際誌

Iori Maeda,Suguru Taniguchi,Yumi Moriuchi,Naruhiko Sawa,Asako Inoue,Tomoyuki Usa,Noriko Watanabe,Keitaro Suyama, Takeru Nose

Peptide Science 2020 ( 日本ペプチド学会 ) 65 - 66 2021年03月

Simple Regulation of the Self-Assembling Ability by Multimerization of Elastin-Derived Peptide (FPGVG) <inf>n</inf>Using Nitrilotriacetic Acid as a Building Block 査読有り

Suyama K., Mawatari M., Tatsubo D., Maeda I., Nose T.

ACS Omega 6 ( 8 ) 5705 - 5716 2021年03月

記述言語：英語掲載種別：研究論文（学術雑誌）

Elastin comprises hydrophobic repetitive sequences, such as Val-Pro-Gly-Val-Gly, which are thought to be important for the temperature-dependent reversible self-association (coacervation). Elastin and elastin-like peptides (ELPs), owing to their characteristics, are expected to be applied as base materials for the development of new molecular tools, such as drug-delivery system carrier and metal-scavenging agents. Recently, several studies have been reported on the dendritic or branching ELP analogues. Although the topological difference of the branched ELPs compared to their linear counterparts may lead to useful properties in biomaterials, the available information regarding the effect of branching on molecular architecture and thermoresponsive behavior of ELPs is scarce. To obtain further insight into the thermoresponsive behavior of branched ELPs, novel ELPs, such as nitrilotriacetic acid (NTA)-(FPGVG)n conjugates, that is, (NTA)-Fn analogues possessing 1-3 (FPGVG)n (n = 3, 5) molecule(s), were synthesized and investigated for their coacervation ability. Turbidity measurement of the synthesized peptide analogues revealed that (NTA)-Fn analogues showed strong coacervation ability with various strengths. The transition temperature of NTA-Fn analogues exponentially decreased with increasing number of residues. In the circular dichroism measurements, trimerization did not alter the secondary structure of each peptide chain of the NTA-Fn analogue. In addition, it was also revealed that the NTA-Fn analogue possesses one peptide chain that could be utilized as metal-scavenging agents. The study findings indicated that multimerization of short ELPs via NTA is a useful and powerful strategy to obtain thermoresponsive molecules.

DOI： 10.1021/acsomega.0c06140

Scopus

その他リンク： https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85104330108&origin=inward

Concentration dependent coacervation peoperty of nonlinear elastin-derived peptide (FPGVG)n analogs 査読有り国際誌

Keitaro Suyama,Mika Mawatari,Daiki Tatsubo,Iori Maeda,Takeru Nose

Peptide Science 2019 ( 日本ペプチド学会 ) 29 - 30 2020年02月

Stability of Phe-containing elastin-like peptides against proteases in digestive organspeptide (FPGVG)n analogs 査読有り国際誌

Iori Maeda,Miki Kawakami,Suguru Taniguchi,Keitaro Suyama,Takeru Nose

Peptide Science 2019 ( 日本ペプチド学会 ) 161 - 162 2020年02月

Development of liposome-like nanostructures composed of short amphiphilic elastin-like peptidestide (FPGVG)n analogs 査読有り国際誌

Naoki Sakamoto,Daiki Tatsubo,Keiji Sato,Keisuke Tomohara,Keitaro Suyama,Iori Maeda,Takeru Nose

Peptide Science 2019 ( 日本ペプチド学会 ) 113 - 114 2020年02月

Enhancement of Self-Aggregation Properties of Linear Elastin-Derived Short Peptides by Simple Cyclization: Strong Self-Aggregation Properties of Cyclo[FPGVG]<inf>n</inf>, Consisting only of Natural Amino Acids 査読有り

Suyama K., Tatsubo D., Iwasaki W., Miyazaki M., Kiyota Y., Takahashi I., Maeda I., Nose T.

Biomacromolecules 19 ( 8 ) 3201 - 3211 2018年08月

記述言語：英語掲載種別：研究論文（学術雑誌）

Elastin-like peptides (ELPs) 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 thermoresponsive materials. Further fundamental studies evaluating coacervative properties of novel nonlinear ELPs could present design concepts for new thermoresponsive materials. In this study, we prepared novel ELPs, cyclic (FPGVG)n (cyclo[FPGVG]n, n = 1-5), and analyzed their 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.

DOI： 10.1021/acs.biomac.8b00353

Scopus

その他リンク： https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85049214569&origin=inward

Angiotensin I converting enzyme-inhibiting peptides purified from elastase-degraded elastin prepared from pig aorta 査読有り

Maeda I., Kai S., Taniguchi S., Inoue A., Li H., Kesamaru H., Nose T.

Current Enzyme Inhibition 14 ( 1 ) 67 - 74 2018年04月

担当区分：責任著者記述言語：英語掲載種別：研究論文（学術雑誌）

Background: Many peptides are produced from food proteins during the manufacturing of various functional foods; unexpected and valuable physiological activities are frequently identified in such released peptides. Elastin, which normally exists as an insoluble elastic fiber, is being used as a new health food material in accordance with the progress in solubilization techniques for elastin. Objective: To evaluate the usefulness of elastin as a material for functional foods, we prepared highly pure, water-soluble elastin from pig aorta and evaluated its angiotensin-converting enzyme (ACE)-inhibitory activity. Method: Pure, water-soluble elastin was prepared from pig aorta using a hydrolyzing method employing a hot alkali reagent. Efficient enzymatic degradation of the elastin was achieved by using elastase that is specific for elastin. The ACE-inhibitory activities of elastin and of peptides obtained via enzymatic degradation were investigated. Three novel ACE-inhibiting peptides were purified from the degradation, and we investigated their ACE-inhibitory activities. Results: Highly pure, water-soluble elastin was prepared from pig aorta; this elastin preparation showed weak inhibitory activity (8.4% inhibition) against ACE. Surprisingly, 6-fold greater enzyme-inhibitory activity was observed for elastin peptides obtained from elastase-mediated degradation of the soluble elastin (48.0% inhibition). Among the enzymatically degraded elastin peptides, three were purified and their primary structures were newly characterized as Val-Tyr-Pro-Gly, Val-Gly-Val-Ala-Pro-Gly, and Gly-Tyr-Pro-Ile. All three peptides showed apparent ACE-inhibitory activity, and Val-Tyr-Pro-Gly exhibited the highest inhibitory capacity among them (60.6% inhibition). Conclusion: These results suggest that water-soluble elastin may serve as a functional food to exert a blood pressure-lowering effect in the body.

DOI： 10.2174/1573408013666170912113121

Scopus

その他リンク： https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85045381253&origin=inward

Stepwise Mechanism of Temperature-Dependent Coacervation of the Elastin-like Peptide Analogue Dimer, (C(WPGVG)<inf>3</inf>)<inf>2</inf> 査読有り

Tatsubo D., Suyama K., Miyazaki M., Maeda I., Nose T.

Biochemistry 57 ( 10 ) 1582 - 1590 2018年03月

記述言語：英語掲載種別：研究論文（学術雑誌）

Elastin-like peptides (ELPs) are distinct, repetitive, hydrophobic sequences, such as (VPGVG)n, that exhibit coacervation, the property of reversible, temperature-dependent self-association and dissociation. ELPs can be found in elastin and have been developed as new scaffold biomaterials. However, the detailed relationship between their amino acid sequences and coacervation properties remains obscure because of the structural flexibility of ELPs. In this study, we synthesized a novel, dimeric ELP analogue (H-C(WPGVG)3-NH2)2, henceforth abbreviated (CW3)2, and analyzed its self-assembly properties and structural factors as indicators of coacervation. Turbidity measurements showed that (CW3)2 demonstrated coacervation at a concentration much lower than that of its monomeric form and another ELP. In addition, the coacervate held water-soluble dye molecules. Thus, potent and distinct coacervation was obtained with a remarkably short sequence of (CW3)2. Furthermore, fluorescence microscopy, dynamic light scattering, and optical microscopy revealed that the coacervation of (CW3)2 was a stepwise process. The structural factors of (CW3)2 were analyzed by molecular dynamics simulations and circular dichroism spectroscopy. These measurements indicated that helical structures primarily consisting of proline and glycine became more disordered at high temperatures with concurrent, significant exposure of their hydrophobic surfaces. This extreme change in the hydrophobic surface contributes to the potent coacervation observed for (CW3)2. These results provide important insights into more efficient applications of ELPs and their analogues, as well as the coacervation mechanisms of ELP and elastin.

DOI： 10.1021/acs.biochem.7b01144

Scopus

その他リンク： https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85043693562&origin=inward

Effects of Salts and pH on Coacervation of Short Elastin-Like Peptide (FPGVG)5 査読有り

Daiki Tatsubo, Misako Kodama, Keiji Sato, Keitaro Suyama, Iori Maeda, and Takeru Nose

Peptide Science 2017 62 - 63 2018年03月

血管の柔軟性を保つには弾力性を生む繊維成分「エラスチン」の補給も重要で牛スジ・豚ハツで補え

前田　衣織

わかさ ( （株）わかさ出版 ) ( 1月 ) 52 - 54 2018年01月

担当区分：責任著者記述言語：日本語掲載種別：記事・総説・解説・論説等（商業誌、新聞、ウェブメディア）

血管の柔軟性を保つには弾力性を生む繊維成分「エラスチン」が重要であることについて、一般の読者へ向けて解説した。エラスチンが血圧降下に作用する可能性があることを示す学術報告を行うことも述べた。

Multifunctional biological activities of water extract of housefly larvae (Musca domestica) 査読有り

Li H., Inoue A., Taniguchi S., Yukutake T., Suyama K., Nose T., Maeda I.

PharmaNutrition 5 ( 4 ) 119 - 126 2017年12月

担当区分：責任著者記述言語：英語掲載種別：研究論文（学術雑誌）

Many types of insects have been used as foods and protein sources. In this study, we investigated the usefulness of housefly larvae (Musca domestica) based on their amino acid composition and multifunctional biological activities. First, the utility of the amino acid composition of housefly larvae was evaluated by amino acid analysis. Notably, the housefly larvae contained sufficient amounts of all essential amino acids, and the amino acid composition was similar to that of hen eggs. Second, we prepared housefly larvae water extract (HLWE) using the decoction method and explored the biological activities of the extract for potential application of the extract as a functional food. HLWE showed significant antioxidant activity (75.4% at 5.00 mg/mL), angiotensin-I-converting enzyme (ACE) inhibitory activity (half-maximal inhibitory concentration [IC50] = 0.430 mg/mL), and dipeptidyl peptidase-IV (DPP-IV) inhibitory activity ([IC50] = 3.52 mg/mL). We found that the low-molecular-weight constituents (<6 kDa) in HLWE contributed to antioxidant and ACE-inhibitory activities, whereas the high-molecular-weight constituents (>6 kDa) contributed to DPP-IV inhibition. Our results suggested that housefly larvae may provide a useful source of multifunctional protein.

DOI： 10.1016/j.phanu.2017.09.001

Scopus

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Coacervation Property and Structural Analysis of Cyclic Analogs of Elastin-derived Peptide (FPGVG)n 査読有り

Keitaro Suyama, Daiki Tatsubo, Hitoshi Kesamaru, Iori Maeda, and Takeru Nose

Peptide Science 2016 101 - 102 2017年04月

Study of Coacervation and Structural Analysis of Short Elastin-Derived Peptides Containing Phenylalanine 査読有り

Mariya Shimai, Suguru Taniguchi, Noriko Watanabe, Asako Inoue, Takeru Nose and Iori Maeda

Peptide Science 2016 231 - 232 2017年04月

Study of Coacervation Ability of Short Elastin-derived Peptide Analogues Using Hydrophobic and Aromatic Amino Acids 査読有り

Suguru Taniguchi, Noriko Watanabe, Asako Inoue, Takeru Nose, and Iori Maeda

Peptide Science 2016 229 - 230 2017年04月

Structural basis of cucumisin protease activity regulation by its propeptide 査読有り

Sotokawauchi A., Kato-Murayama M., Murayama K., Hosaka T., Maeda I., Onjo M., Ohsawa N., Kato D., Arima K., Shirouzu M.

Journal of Biochemistry 161 ( 1 ) 45 - 53 2017年01月

記述言語：英語掲載種別：研究論文（学術雑誌）

Cucumisin [EC 3.4.21.25], a subtilisin-like serine endopeptidase, was isolated from melon fruit, Cucumis melo L. Mature cucumisin (67 kDa, 621 residues) is produced by removal of the propeptide (10 kDa, 88 residues) from the cucumisin precursor by subsequence processing. It is reported that cucumisin is inhibited by its own propeptide. The crystal structure of mature cucumisin is reported to be composed of three domains: the subtilisin-like catalytic domain, the protease-associated domain and the C-terminal fibronectin-III-like domain. In this study, the crystal structure of the mature cucumisin•propeptide complex was determined by the molecular replacement method and refined at 1.95 Å resolution. In this complex, the propeptide had a domain of the α-β sandwich motif with four-stranded antiparallel β-sheets, two helices and a strand of the C-terminal region. The β-sheets of the propeptide bind to two parallel surface helices of cucumisin through hydrophobic interaction and 27 hydrogen bonds. The C-terminus of the propeptide binds to the cleft of the active site as peptide substrates. The inhibitory assay suggested that the C-terminal seven residues of the propeptide do not inhibit the cucumisin activity. The crystal structure of the cucumisin•propeptide complex revealed the regulation mechanism of cucumisin activity.

DOI： 10.1093/jb/mvw053

Scopus

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Investigation of water-soluble elastin as a multifunctional cosmetic material:　 moisturizing and whitening effects 査読有り

Asako Inoue, Tomohiro Hikima, Suguru Taniguchi, Takeru Nose, Iori Maeda

J. Cosmetc Sci. 68 ( 1 ) 11 - 24 2017年01月

Investigation of water-soluble elastin as a multifunctional cosmetic material: Moisturizing and whitening effects 査読有り

Inoue A., Hikima T., Taniguchi S., Nose T., Maeda I.

Journal of Cosmetic Science 68 ( 1 ) 11 - 23 2017年01月

担当区分：責任著者記述言語：英語掲載種別：研究論文（学術雑誌）

Elastin and collagen are extracellular matrix proteins that are widely distributed in the body. Although elastin essentially functions as a skin moisturizer, there have been few reports on its other fundamental chemical and biological functions. In this study, we investigated the moisturizing and whitening (tyrosinase inhibition) effects of elastin to examine its usefulness as a cosmetic material. Water-soluble hot alkali pig aorta (HAPA)- elastin was prepared from pig aorta using the hot alkali method. HAPA-elastin showed a widely distributed molecular weight and had a coacervation property that mediated reversible self-assembly of its molecules with increasing temperature. Amino acid analysis of HAPA-elastin showed a high content (81.5%) of hydrophobic amino acids such as Gly, Ala, Val, and Pro. Des (desmosine) and Ide (isodesmosine), which are characteristic amino acids of elastin, accounted for more than 0.4% of the total amino acid content. HAPA-elastin showed a moisture-retaining property. The water content of skin samples treated with and without HAPA-elastin was 77.2% ± 7.8% and 49.4% ± 10.1%, respectively. HAPA-elastin also inhibited tyrosinase activity by 11.3% ± 3.9%. The results obtained indicate that elastin has a useful function as a cosmetic material.

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Identification of an Elastin-derived Peptide Degradate in Human Blood After Oral Ingestion of Elastin 査読有り

Iori Maeda, Suguru Taniguchi and Takeru Nose

Peptide Science 2015 305 - 306 2016年04月

Dimerization effects on coacervation property of an elastin-derived synthetic peptide (FPGVG)<inf>5</inf> 査読有り

Suyama K., Taniguchi S., Tatsubo D., Maeda I., Nose T.

Journal of Peptide Science 22 ( 4 ) 236 - 243 2016年04月

記述言語：英語掲載種別：研究論文（学術雑誌）

Elastin, a core protein of the elastic fibers, exhibits the coacervation (temperature-dependent reversible association/dissociation) under physiological conditions. Because of this characteristic, elastin and elastin-derived peptides have been considered to be useful as base materials for developing various biomedical products, skin substitutes, synthetic vascular grafts, and drug delivery systems. Although elastin-derived polypeptide (Val-Pro-Gly-Val-Gly)n also has been known to demonstrate coacervation property, a sufficiently high (VPGVG)n repetition number (n > 40) is required for coacervation. In the present study, a series of elastin-derived peptide (Phe-Pro-Gly-Val-Gly)5 dimers possessing high coacervation potential were newly developed. These novel dimeric peptides exhibited coacervation at significantly lower concentrations and temperatures than the commonly used elastin-derived peptide analogs; this result suggests that the coacervation ability of the peptides is enhanced by dimerization. Circular dichroism (CD) measurements indicate that the dimers undergo similar temperature-dependent and reversible conformational changes when coacervation occurs. The molecular dynamics calculation results reveal that the sheet-turn-sheet motif involving a type II β-turn-like structure commonly observed among the dimers and caused formation of globular conformation of them. These synthesized peptide dimers may be useful not only as model peptides for structural analysis of elastin and elastin-derived peptides, but also as base materials for developing various temperature-sensitive biomedical and industrial products.

DOI： 10.1002/psc.2876

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Dimerization effects on coacervation property of an elastin-derived synthetic peptide (FPGVG)5. 査読有り

Keitaro Suyama , Suguru Taniguchi, Daiki Tatsubo, Iori Maeda, Takeru Nose

Journal of Peptide Science 22 ( 4 ) 236 - 243 2016年04月

Development of short and highly potent self-assembling elastin-derived pentapeptide repeats containing aromatic amino acid residues 査読有り

Suguru Taniguchi, Noriko Watanabe,Takeru Nose, and Iori Maeda

Journal of Peptide Science 22 ( 1 ) 36 - 42 2016年01月

Design of phenylalanine-containing elastin-derived peptides exhibiting highly potent self-assembling capability 査読有り

Maeda I., Taniguchi S., Watanabe N., Inoue A., Yamasaki Y., Nose T.

Protein and Peptide Letters 22 ( 10 ) 934 - 939 2015年08月

担当区分：責任著者記述言語：英語掲載種別：研究論文（学術雑誌）

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.

DOI： 10.2174/092986652210150821170703

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Design of Phenylalanine-Containing Elastin-Derived Peptides Exhibiting Highly Potent Self-Assembling Capability. 査読有り

Iori Maeda, Suguru Taniguchi, Noriko Watanabe, Asako Inoue, Yuko Yamasaki and Takeru Nose

Protein & Peptide Letters 22 ( 10 ) 934 - 939 2015年08月

Comparison between Coacervation Property and Secondary Structure of Synthetic Peptides, Ile-containing Elastin-derived Pentapeptide Repeats 査読有り

Iori Maeda, Suguru Taniguchi, Junko Ebina, Noriko Watanabe, Takao Hattori, and Takeru Nose

Protein & Peptide Letters 20 ( 8 ) 905 - 910 2013年08月

美肌実現には肌の弾力性分エラスチンが不可欠で補ったら小ジワタルミが薄れた！肌はプルプル！

前田　衣織

わかさ ( （株）わかさ出版 ) ( 6月 ) 140 - 141 2013年06月

第2は血管の柔軟性アップで血管の弾力性分エラスチンの補給がよく効き血圧は上も下も下がりスジ肉で補え

前田　衣織

わかさ ( （株）わかさ出版 ) ( 2月 ) 38 - 39 2013年02月

５０代までに半減する血管の弾力線維エラスチンを毎日少し補えば高血圧が下がり血管年齢も続々若やぐ

前田　衣織

わかさ ( （株）わかさ出版 ) ( ６月 ) 91 - 92 2012年06月

春の美肌作りにはコラーゲンよりも肌のゴム線維エラスチンこそ必要で小ジワタルミが消えた！１０歳若返った！

前田　衣織

わかさ ( （株）わかさ出版 ) ( ５月 ) 122 - 123 2012年05月

エラスチン由来Ile含有ペンタペプチドの二次構造解析査読有り

渡邊法子,谷口卓,前田衣織

北九州医工学術者協会誌 2012年03月

Structural requirements essential for elastin coacervation: Favorable spatial arrangements of valine ridges on the three-dimensional structure of elastin-derived polypeptide (VPGVG)n 査読有り

Iori Maeda, Yoshiteru Fukumoto, Takeru Nose, Yasuyuki Shimohigashi, Takashi Nezu, Yoshihiro Terada, Hiroaki Kodama, Kozue Kaibara, and Kouji Okamoto

Journal of Peptide Science 17 ( 11 ) 735 - 743 2011年11月

Structural analysis and coacervation properties of Ile-containing elastin-derived pentapeptide analogues 査読有り

Suguru Taniguchi, Noriko Watanabe, Junko Ebina, Kaori Oka, Kouji Okamoto, and Iori Maeda

PEPTIDE SCIENCE 2010 146 - 146 2011年03月

Elastin peptides prepared from piscine and mammalian elastic tissues inhibit collagen-induced platelet aggregation and stimulate migration and proliferation of human skin fibroblasts 査読有り

Eri Shiratsuchi,Megumi Ura,Misako Nakaba,Iori Maeda,Kouji Okamoto

J. Pept. Sci. 16 652 - 658 2010年09月

Involvement of fibronectin and matrix metalloproteinases in airway smooth muscle cell migration for the process of airway remodeling. 査読有り

Machiko Nishihara-Fujiwara,Shunsuke Shoji,Iori Maeda,Terufumi Shimoda,Sankei Nishima,Kouji Okamoto

Allergol. Int. 59 267 - 275 2010年09月

NMR study on a considerable difference between temperature-dependent molecular assembly and disassembly processes of elastin-like polypentapeptide 査読有り

Shinsuke Hirai,Keiko Ideta,Suguru Taniguchi,Eri Shiratsuchi,Iori Maeda,Kouji Okamoto

Peptide Science 2009 391 - 392 2010年03月

魚類及び哺乳類由来水溶性エラスチンの比較とその応用査読有り

白土絵理,中場操子,前田衣織,岡元孝二

九州医工学術者協会誌 19 19 - 22 2009年04月

Two types of cation binding sites on elastomeric polypeptides:effects on self-assembly process and elastomeric functions 査読有り

Akihiko Okajima,Yuji Tanaka,Junko Kuwahara,Masayuki Naito,Iori Maeda,Kouji Okamoto,Kozue Kaibara

Peptide Science 2008 505 - 508 2009年03月

Analysis of coacervation properties of Ile-containing elastin-derived pentapeptide analogues 査読有り

Iori Maeda,Junko Ebina,Suguru Taniguchi,Amchiko Nishihara,Eri Shiratsuchi,Kaori Oka,Kouji Okamoto

Peptide Science 2008 289 - 292 2009年03月

エラスチン由来ペプチドの構造とコアセルベーション特性査読有り

前田衣織,岡元孝二

Jasco Report 50 1 - 5 2008年09月

Characterization of the Molecular Interaction between Tropoelastin and DANCE-Fibulin-5 査読有り

Hiroshi Wachi,Risa Nonaka,Fumiaki Sato,Kayoko Shibata-Sato,Marie Ishida,Saori Iketani,Iori Maeda,Koji Okamoto,Zsolt Urban,Satosh Onouei,Yoshiyuki Seyama

J. Biochem 143 ( 5 ) 633 - 639 2008年04月

Structural profiles for coacervation of elastin-derived polypeptides 査読有り

Iori Maeda,Yoshiteru Fukumoto,Takeru Nose,Yasuyuki Shimohigashi,Takashi Nezu,Yoshihiro Terada,Hiroaki Kodama,Kozue Kaibara,Kouji Okamoto

Peptide Science 2007 219 - 222 2008年03月

平成１９年度日本ペプチド学会奨励賞を受賞して

前田　衣織

PEPTIDE NEWS LETTER JAPAN 67 5 - 8 2008年01月

Immunochemical and immunohistochemical studies on distribution of elastin fibers in human atherosclerotic lesions using a polyclonal antibody to elastin-derived hexapeptide repeat 査読有り

Iori Maeda,Sonoko Kishita,Yuji Yamamoto,Kazunari Arima,Keiko Ideta,Jing Meng,Noriyuki Sakata,Kouji Okamoto

the Journal of Biochemistry 142 ( 5 ) 627 - 631 2007年11月

Induction of macrophage migration through lactose-insensitive receptor by elastin-derived nonapeptides and their analogue 査読有り

Iori Maeda,Noriaki Mizoiri,Maria Portia P. Briones,Kouji Okamoto

Journal of Peptide Science 13 ( 4 ) 263 - 268 2007年04月

Domains 16 and 17 of Tropoelastin in Elastic Fiber Formation 査読有り

Hiroshi Wachi,Fumiaki Sato,Junji Nakazawa,Risa Nonaka,Zoltan Szabo,Zsolt Urban,Takuo Yasubaga,Iori Maeda,Koji Okamoto,Barry C Starcher,Dean Y Li,Robert P Mecham,Yoshiyuki Seyama

Biochemical Journal 402 63 - 67 2007年04月

Nanoparticles from elastin-based polymers as drug release devices 査読有り

Kouji Okamoto ,Asami Doi,Shuichiroh Uehara,Eri Shiratsuchi,Maria Portia P. Briones,Iori Maeda,Masakazu Furuta

Understanding Biology Using Peptides, (E. Escher, W.D. Lubell and S.D. Valle Ed.) 611 - 611 2006年07月

Nanoparticles preparation using elastin-derived polypeptide and co-polypeptide for design of drug release devices 査読有り

Asami Doi,Iori Maeda,Masakazu Furuta,Kouji Okamoto

Peptide Science 2005 281 - 282 2006年03月

ペプチド大好き

前田　衣織

PEPTIDE NEWS LETTER JAPAN 59 3 - 4 2006年01月

Synthesis and Coacervation Property of Elastin-derived Val-, Phe, Ala, and/or Lys-containing Copolymers for Design of Drug Release Devices 査読有り

Shuichiroh Uehara,Masashi Yamashita,Iori Maeda,Kouji Okamoto,Masakazu afuruta,Masamichi Iwama

Peptide Science 2004 389 - 390 2005年02月

Chemotactic and Proliferative Reseponses of Vascular Smooth Muscle Cells to Elastin-derived Peptides 査読有り

Iori Maeda,YoheiYamada,Machiko Nishihara,Kouji Okamoto

Peptide Science 2004 483 - 484 2005年02月

Macrophage Chemotactic Activity-structure Relationship of Elastin-derived Nonapeptides 査読有り

Noriaki Mizoiri,Maria Portia P. Briones,Iori Maeda,Kouji Okamoto

Peptide Science 2003 323 - 324 2004年01月

Elastin-derived Peptides: Structures, Functions and Mechanisms 査読有り

Iori Maeda,Maria Portia P. Briones,Machiko Nishihara,Hiroaki Kodama,Michio Kondo,Takashi Nezu,Yoshihiro Terada,Kouji Okamoto

Peptide Science 2003 31 - 34 2004年01月

Extracellular Matrix Components Induce Chemotaxis of Airway Smooth Muscle Cells in the Process of Airway Wall Remodeling 査読有り

Machiko Nishihara,Iori Maeda,Shunsuke Shoji,Kouji Okamoto

北九州医工学術者協会誌 14 ( 1 ) 39 - 42 2003年06月

Structural Analyses of Elastin-derived Peptide Analogues 査読有り

Iori Maeda,Takashi Nezu,Yoshihiro Terada,Kouji Okamoto

Peptide Science 2002 349 - 350 2003年03月

Possible Involvement of Increased Glycoxidation and Lipid Peroxidation of Elastin in Atherogenesis in Haemodialysis Patients 査読有り

Yuji Yamamoto,Noriyuki Sakata,Jing Meng,Masaya Sakamoto,Akiko Noma,Iori Maeda,Kouji Okamoto,Shigeo Takebayashi

Nephrol. Dial. Transplant. 17 630 - 636 2002年08月

Coacervation properties of elastin-derived polypeptides and structural analyses 査読有り

Iori Maeda,Yoshiteru Fukumoto,Michio Kondo,kozue Kaibara,Kouji Okamoto

Peptide Science 2001 285 - 286 2002年03月

Conformational analysis and preparation of polyclonal antibody for the domain 26A of human elastin 査読有り

Kumiko Takeshita,Takeshi Matsui,Yoshito Ueki,Iori Maeda,Jing Meng,Noriyuki Sakata,Kouji Okamoto

Peptide Science 2001 225 - 226 2002年03月

Interaction of solution and solid states of elastin-derived peptides with contractile and synthetic phenotypes of vascular smooth muscle cells 査読有り

Kouji Okamoto,Kaoru Taira,Rie Kikugawa,Kyoko Kotsuru,Eiichi Hirano,Iori Maeda

Peptide Science 2001 123 - 126 2002年03月

Coacervation and Conformational Studies of Elastin-derivedPolypeptide (VPGVG)n and Its Analogues 査読有り

Iori Maeda,Yoshiteru Fukumoto,Kouji Okamoto,Kozue Kaibara,Michio Kondo

Proceedings of "The 4th International Symposium on Frontiers in Protein Chemistry and Biotechnology" 6 - 7 2001年08月

Coacervation and CD and FT-IR spectroscopic studies of elastin-derived polypentapeptide and its analogs 査読有り

Kouji Okamoto,Yoshiteru Fukumoto,Iori Maeda,Elemer Vass,Zsuzsanna Majer,Gabor Dibo,Miklos Hollosi

Peptides: The Wave of the Future (M. Lebl & R. A. Houghten, eds) 336 - 337 2001年06月

Macrophage chemotactic response to elastin-derived VGVAPG and VGVPG permutations: A structure-activity relastionship and receptor binding assay 査読有り

Maria Portia P. Briones,Satsuki Kamisato,Iori Maeda,Noboru Takami,Kouji Okamoto

Peptides: The Wave of the Future (M. Lebl & R. A. Houghten, eds) 807 - 808 2001年06月

Macrophage chemotaxis induced by elastin-desrived hexapeptides and its signal transduction mechanism 査読有り

Kouji Okamoto,Maria Portia P. Briones,Satsuki Kamisato,Iori Maeda,Noboru Takami

Peptides 2000 701 - 702 2001年05月

Comparison of Chemotactic Activity of Macrophages Induced by Permutations of Elastin-derived Hexapeptide VGVAPG and Pentapeptide VGVPG 査読有り

Maria Portia P. Briones,Kyoko Kozuru,Iori Maeda,Satsuki Kamisato,Noboru Takami (Fukuoka Univ.),Kouji Okamoto

Peptide Science 2000 255 - 258 2001年04月

Elastin-derived Polypeptides, (VPGVG)n, (VPGV)n and (VPG)n: Coacervation Property and Specific Interaction with Metal Ions 査読有り

Yoshiteru Fukumoto,Iori Maeda,Kouji Okamoto,Kozue Kaibara (Kyushu Univ.),Michio Kondo (Saga Univ.)

Peptide Science 2000 189 - 192 2001年04月

Preparation of polyclonal antibody against elastin hexapeptide sequence and its recognition site 査読有り

Iori Maeda,Sonoko Kishita,Keiko Ideta,Kazunari Arima,Jing Meng,Noriyuki Sakata,Kouji Okamoto

Peptide Science1999 217 - 220 2000年04月

Chemotactic activation of macrophages by elastin hexapeptide sequences and its signaling mechanism 査読有り

Maria Portia P. Briones,Iori Maeda,Satsuki Kamisato,Noboru Takami(Fukuoka Univ.),Kouji Okamoto

Peptide Science 1999 221 - 224 2000年04月

Effects of selective metal ion binding on structural and functional characteristics of elastin peptides 査読有り

Kozue Kaibara (kyushu Univ.),Tohru Watanabe,Yoshiteru Fukumoto,Iori Maeda,Kouji Okamoto

Peptide Science 1999 263 - 266 2000年04月

The effect of elastin peptides on cell migration in cultured chick vascular smooth muscle cells 査読有り

Rie Kikugawa,Kaoru Taira,Eiichi Hirano,Iori Maeda,Kouji Okamoto

Peptide Science 1999 225 - 228 2000年04月

Structural Essentials for Novel Inhibition of Serine Proteinase Chymotrypsin 査読有り

Yasuyuki Shimohigashi,Yasuko Yamauchi,Koichi Ikesue,Iori Maeda,Megumi Kawahara,Takeru Nose

Peptide Science-Present and Future 　 ( 　 ) 649 - 651 1999年04月

Design of Serine Protease Inhibitors with Conformation Restricted by Amino Acid Side-Chain-Side-Chain CH/π Interaction 査読有り

Yasuyuki Shimohigashi,Takeru Nose,Yasuko Yamauchi,Iori Maeda

Biopolymers 51 9 - 17 1999年04月

Identification of a novel analgesic petide including an unnatural aminoacid from peptide libraries synthesized with a multipeptide synthesizer 査読有り

前田　衣織

Peptide Science-Present and Future 139 - 140 1999年04月

X-ray Crystal Structure of a Dipeptide-Chymotrypsin Complex in an Inhibitory Interaction 査読有り

Akiko Kashima,Yoshihisa Inoue,Naritoshi Sugio,Iori Maeda,Takeru Nose,Yasuyuki Shimohigashi

European Journal of Biochemistry 255 12 - 23 1998年04月

Purification and characterization of a cellulase from the giant snail Achatina fulica 査読有り

前田　衣織

Bioscience, Biotecnology and Biochemistry 60 ( 1 ) 122 - 124 1996年04月

Chymotrypsin inhibitory conformation induced by amlno acid side chain-side chain intramolecular CH/π interaction 査読有り

前田　衣織

Journal of Chemical Society, Perkin Trans 1 2479 - 2485 1996年04月

Chymotrypsin inhibition induced by side chain-side chain intramolecular CH/π interaction in D-Thr-L-Phe bengylamide 査読有り

前田　衣織

Journal of Biochemistry 119 870 - 877 1996年04月

water-soluble chymotrypsin specific inhibitors containing arginine 査読有り

前田　衣織

Biochemical and Biophisical Research Communications 193 ( 1 ) 428 - 433 1993年04月

Characterization of peptides isolated from Trimeresurus flavoviridis and Trimeresurus ok navensis venoms 査読有り

前田　衣織

Bulletin of the chemical society of Japan 66 ( 5 ) 1569 - 1571 1993年04月

Chymotrypsin inhibitory conformation of dipeptides constructed by side chain hydrophobic interactions 査読有り

前田　衣織

Journal of Molecular Recognition 6 ( 2 ) 95 - 100 1993年04月

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