研究者詳細 - 前田　衣織

論文 - 前田　衣織

分割表示94 件中 21 - 40 件目／全件表示 >>

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

その他リンク： https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85030256505&origin=inward

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

その他リンク： https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85014580285&origin=inward

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.

Scopus

その他リンク： https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85044740990&origin=inward

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

Scopus

その他リンク： https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=84962421662&origin=inward

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

Scopus

その他リンク： https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=84940830108&origin=inward

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

　前のページ - 次のページ　

<前田 衣織>

論文 - 前田 衣織

<前田　衣織>

論文 - 前田　衣織